ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9KDJ3 | MNVFDTLQQSKKLPDVYRQMTRVELEERIRQHKERLGKKLLMLGHHYQRDEVFQFADQTGDSLQLAQIAAKEKEAQFIVFCGVHFMAETADLLTSEEQTVLLPDLRAGCSMADMADIHQTERAWERLQLMFGDTILPLTYVNSTAAIKAFCGRNGGATVTSSNAKKMLEWAFTQKERLLFLPDQHLGRNTAYELGIPLEAMAVWNPETERLETDQPLENIRVILWKGHCSVHEKFTVKHIEHLRKNEPDMSIIVHPECTHDVVIHADDAGSTHYIIKTIESADSGTKWAVGTEMNLVNRLANEHPDKEIVSLNPTMCPCLTMNRIDIEHLCWSLDQLAEGVFQHPIKVEDKDRGPALLALQRMLDRA | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 41873
Sequence Length: 367
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.72
|
Q5UXB3 | METAAFETDLSLFKYDNLEQLPPSYRDLDADERTERIESALAELGDDVVILGHNYQRQEIVEHADFIGDSYQLSKEAAQSDADYVIFGGVTFMAESADIITDDDQSVILPSMEASCPMAGMAEALQVDAAWAELTAALDDEEIIPITYMNSYADLKAFCAEQGGLVCTSSNAHKAFEYAFEKGDKVLFLPDKHLGENTAHRLGMADETVEWDPWDAEGTDAADAVENDVILWEGYCQVHERFREHHIESIREDYPDANVIVHPECRREVVEAADVAGSTSTICESVAEADPGETWAIGTEIHLTHHLQRWHPDVNVVPLCGDACMDCNAMRQIDPNYLAWVLEELVEGRERNVIEVAPEEKELAQVAMDRMLEI | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 41761
Sequence Length: 374
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.72
|
Q9F364 | MTTAQTQELDVQPTPLALLLLGREADPRSERGVECPGDLPSPSDPDLVARARAAKEKLGDKVFVLGHHYQRDEVIQFADVTGDSFKLARDAAARPEAEYIVFCGVHFMAESADILTSNDQKVVLPDLAAGCSMADMATAEQVAECWDVLTEAGIAEQVVPVSYMNSSADIKAFTGKHGGTICTSSNAERALNWAFEQGEKVLFLPDQHLGRNTAVRDLGMSLEDCVVYNPHRPNGGLTAKELRDANMILWRGHCSVHGRFSLDSVNDVRERIPGVNVLVHPECKHEVVAAADYVGSTEYIIKALEAAPAGSKWAIGTELNLVRRLANRFAAEDKEIVFLDKTVCFCSTMNRIDLPHLVWTLESLAEGTLVNRIEVDQETEAFAKLALERMLALP | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 43125
Sequence Length: 394
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.72
|
Q9L790 | MFLAADRPTTDLPADLPAAIAALKQELNAVILAHYYQEAAIQDVADYIGDSLGLSRQAAAADADVIVFAGVHFMAETAKILNPQRQVLLPDLAAGCSLADSCPPEAFAAFKAAHPNHIVISYINCTAEIKALSDIICTSSNAVKIVQQIPVDQPIIFAPDRNLGRYVMQQTGRDLVLWDGSCIVHETFSEQRLLELQARHPDAEIIAHPECETPVLDQARFIGSTTALLNYSLNSPSREFIVVTEPGIIHQMQQAAPEKTFIPAPPQDTTCACNECPFMRLNTLEKLYLCMRDRRPEIQIPEETRLAALRPIERMLAMSA | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 35156
Sequence Length: 320
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.72
|
Q9X1X7 | MVDEILKLKKEKGYIILAHNYQIPELQDIADFVGDSLQLARKAMELSEKKILFLGVDFMAELVKILNPDKKVIVPDRSATCPMANRLTPEIIREYREKFPDAPVVLYVNSTSECKTLADVICTSANAVEVVKKLDSSVVIFGPDRNLGEYVAEKTGKKVITIPENGHCPVHQFNAESIDAVRKKYPDAKVIVHPECPKPVRDKADYVGSTGQMEKIPEKDPSRIFVIGTEIGMIHKLKKKFPDREFVPLEMAVCVNMKKNTLENTLHALQTESFEVILPKEVIEKAKKPILRMFELMG | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 33617
Sequence Length: 298
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.72
|
Q5SJM4 | MGRMRGEALAQEVLRLKRERNAVILAHSYQLPEVQEVADFVGDSLGLAREAQRTRAEVIVFCGVHFMAETAAILNPEKTVLLPDLEAGCSLADSIRPEDVLAWKAKHPDGIVVAYVNTKAEVKALADVCVTSANAVEVVSRLPQDRPIYFVPDMFLGAHVARVTGRRLDLFPGECHVHAGIREEHLKALLEAHPGAEFLIHPECGCGSGCLYLKPDAKMLSTEGMVRYAKGAEAREFVVATEVGILHRLKKEAPEKAFFPVKPDAVCEYMKRITLEKVYLSLKEMRHVVRVPEEVAGRARRALEAMVAVG | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 34181
Sequence Length: 310
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.72
|
B5YJJ2 | MVNRTVEEILALKKQRNAIILAHNYQREEVQEIADFVGDSLELSRQATKVDCDVIVFCGVHFMAETAAILNPDKTVLLPEIDAGCPMADTVDVEELKRWIDRYPYAPIVSYVNTTAEVKALSYACCTSANAPQIVKAVPFSSIIFVPDKNLADWVKKHVPEKDIIAWNGFCPTHHMIKKEDIIRAKKAHPDALVVVHPECRPEVIELADHVASTSGMVRFARAASQKEFIIGTEVGLLYRLKKENPDKVFYPIKKTMICPNMKITTLESILTALKENQYVIKVPEDIRIKAYEAVQRMLTLIS | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 34147
Sequence Length: 303
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.72
|
B3PKM9 | MRPTLGLFGGTFDPIHIGHLRLALELKQQLQLDGMRLMPCHLPAHRDQPGASSTQRATMLQLALAACPELSIDLREVARARASYTVDSLSELRAELGAETSLVFCLGTDSFAGLDRWHRWQELLQLAHLVVVERPGWDIPSTGPVRTLLAQHQGAPGQLRLAACGSIVRLAPRLLPISATEIRQLIGAGQSPQFLVPDSVWQYIGQERLYR | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 23294
Sequence Length: 211
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
A3PLX6 | MVVGLLGGSFDPPHPGHVHITREALKRFGLDRVWWLVSPGNPLKPRPPAPLARRLAEARRLMRHPRVAVTGLEAEIGTRFTAETLAVLQRRYPGVRFVWLMGADNLAQFHRWERWRAIMESVPVGVLARPGAGLRARTSPAARRYASALLPEAEAARLGRSAAPAWCFVNLPMMDLSSTEIRATGRWRGQAD | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 21379
Sequence Length: 192
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
Q3ANY3 | MHCALMGGSFDPPHNGHLALALAARELLNVECLFLSPSRNPFKGESLLDDVHRIQLVELLAKEVNRTGSGCEVCRWEIEQAAPSYTVELISYLTQSYPTWRFTLILGEDNFHSFHLWKEYQEILRLCHVAVFRRSSEAVVPSLDEAMLVQEGVSFYNFDAPLSSTDIRKQLRAGLPVNGLLPASILRYIEQEGLYR | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22221
Sequence Length: 196
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
B3QLU8 | MRTGIFGGSFDPPHNGHLAMCLFARELLRLDRLIVSVSRNPFKTGAHASDDDRVSMARLLTDEVNAAGRFAESSSWELETDGPSYTVDLLRHIADLYPDDELLLLVGEDSYRQMGQWKAASEIPRLCQIVYFGREGYENCQHDAEALHLPVRRIDFDMPVSATEIRRLVAAGQPVSQLVPPSINHYIAEHGLYRS | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 21910
Sequence Length: 195
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
B3EQ84 | MRLAVFGGSFDPPHNGHLALCLYARELLQVDRLVISASNNPLKDAPQAADRDRVKMAELLAETINRTGAFAEVSSWEANRGHPVYTIDLMEYLEEIYSTSDLTLLIGEDNFLNFRQWKSWEELIRRYSIIVFGRKADDGASDDSAISERLHDQSFRHIDLNLPLSSTEIRKRLASGDDCSAEIPSPIWQYIVENQLYQ | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22559
Sequence Length: 198
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
B3QYZ5 | MKKIALFGGSFDPPHYGHFALCTLTRELFSPEKIILSISKNPLKGSANAPEAHQLAMAKLMAEELGKTGPVFEVSDWELRRAGFSYTIETLRHFHAIEPNAELLLCIGEDNYQIFEKWKAYQEILQLAHLVVFARSGTQGEQQSSRIIPPERYTWVQLDLPLSSSDLRREIAEGQDWQAKMPSSIAAHIAAHRLYQNEK | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22562
Sequence Length: 199
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
Q8KGF2 | MRTAVFGGSFDPPHNGHLALSLFARELAGLDRLIVSVSKNPFKAAADASDDDRSAMARLLVAEINVAGVFAEISGWELQQSGPSYTIDLLRHVEERCPGDELVLLVGEDSYLQMPQWKFASEILKHCTIAVFGRSDIDAADAPPSDPLLPAIHYDFDMPVSATKIRRLAAAGQPIGQFVPSSIAQYIAEHKLYSA | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 21163
Sequence Length: 195
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
Q1QXB3 | MCAAEARPARVAMLGGTFDPVHMGHLRSAVELREALELDRVHMVPARVPPHRATPGVSAERRAALLALGIGDTPGLAVDDREIARDGPSYSADTLASLREELGPQARLVMALGHDAYLNLAEWHEPQRLFDLAHIVVIDRPDHDRPLAPALQELVAGREVSDVETLMQAPAGSLLALRLPTRMAISATSIRERLRRGDSIRYLVPEAVERDLLARGLYA | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 23912
Sequence Length: 219
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
Q7P0P7 | MNARVGVFGGTFDPVHHAHLRMARAFADELALDEVRLIPAGQPYHRLEGPHASAAQRLDMVKLAIAADARLAVDEREIRRARPAYTVDTLRELRAELGDAAELWFLIGGDSLAALSSWKDWRKLFRLANLAVAMRPGFDPAALPPEVFQEWQARQVSDFSNRTASGTIRPLALPPLDLSATRLRARLAADEPVDGLIDPAVLAYIRRQRLYR | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 23621
Sequence Length: 212
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
B5EEI3 | MRLGILGGTFNPIHNAHLRIAEEARDLYQLDRVVFIPAATPPHKPLVGELSFASRLEMVRLAVADNPGFMVSDMEGVRGGRSYSIDTLRELKARYPDDDLFFIVGADSFNDISTWREYEAIFELCNVISVQRPGSTITSLAEALPVAIAGEFCYDPAAKRLNHCSGHAVYALDGVLLDISSSHIRLSVQGGRSIRYLLPDAVEHYIKEQRLYVDAR | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 24020
Sequence Length: 216
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
Q49Y35 | MAKSIVLYGGQFNPIHIAHMVVASEVNAFIKPDVFYFIPSFISPLKEHTDYLEGRYRVDMIQSVIDDLGFGRICLNEIERRGQSYTYDTVMYILDKHPDAKLYLVIGTDQYNQLHKWFKINELKSYITFVIVNRDKTTQEVESEMLSITIPRIDISSTLIRKRVKNKENIQALVSPSVEQYIREEGLYES | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22148
Sequence Length: 190
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
Q9RDK7 | MGGTFDPIHHGHLVAASEVAAQFQLDEVVFVPTGQPWQKSHRAVSAAEDRYLMTVVATVENPQFSVSRIDIDRGGPTYTVDTLRDLRALNPDADLFFITGADALAQILTWRDSEELFSLAHFIGVTRPGHTLTDAGLPKGGVSLVEVPALAISSTDCRARVAKGDPVWYLVPDGVVRYIDKRHLYRGE | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 20581
Sequence Length: 188
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
B2FPR4 | MMSLRIYYGGTFDPVHLGHLAIARAARDELQVAVRMLPAADPPHRAVPGATADQRFTMLSLAIGDEPGLLLDHRELDRAIRFPGRPSYTVDTLRELRGELGPSRPLAWLVGADSLLGLTRWHEWEALFGLAHFVVAERPGSPLQASVDGELGRALEGRWADNEQALFASPAGRILRLHHPLREESASAVRAQIAAGGPWRALLPPAVADYVAAHGLYRSPTP | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 24188
Sequence Length: 222
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
Q8DSI6 | MALELLTPFTKVELEEERKDKNRKQIGILGGNFNPVHNAHLLVADQVRQQLGLDEVLLMPEYKPPHVDKKATIDEKHRLKMLELAIKGIEGLAIETIELKRKGVSYTYDTMKDLIEQNPDVDYYFIIGADMVDYLPKWHKIDELIQMVQFVGVQRPKYKAGTSYPVIWVDVPLMDISSSMIRDFIRKNRKPNFLLPKLVLDYIEKEGLYQ | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 24441
Sequence Length: 210
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
Q30PQ2 | MDTIALFGGSFDPPHIGHEAIIEALKKFKDIDKIIIMPTFLNPFKSNFYAPSSLRVKWLREIFKEEKRVEVSDYEVLQNRQVPTIETAKHLLESYKKIYLVIGADNLAKLRDWNSYDELKELVTFVVATRDDIEIPDEFIMLSVDEKISSTQLRENIQLSKLPKKCAKEIYDFYKEEHCKTE | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 21320
Sequence Length: 182
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
A6QCD6 | MVNQSKPEVAIFGGSFDPPHKGHQQIVRKAVQILDIDKLIVLPAYLNPFKNVSLANPEKRLEWCYQLFDGIPKVVVDDYEIRQNKSVRTSQSVKHFNNTYSVKYLIIGSDNLSTLTKWHEFKWLNDHITWVIVTRKGHPVQTEGLKSWRILEIDFPISSTTIREKKDLRYIDNKIKQSVEKTIKDKKE | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 21959
Sequence Length: 188
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
Q67SC4 | MARVAVLGGTFDPIHLGHLAAAQGVLHLTGVERVIFLPNRQPPHKQGQPVTPAEHRAAMVRLAIADNPAFGFSDLELRRPGPSYTIETVRALAAEHPDWEPAFIIGLDSLLAIRTWREWETLMQSVDFFAVTRPGHDLAAARRLLAELGPRLSGRVRLLEIPGVAVASADLRRLAAAGYPLRYLVPDPVARYIAEHRLYLRGESHGDG | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22845
Sequence Length: 208
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
|
Q8TK88 | MDFEKAQNRIIEFIRNETDKAGVDGAVVGISGGIDSALTATLTVEALGKERVLGLHMPESSLTPAVDSEDAKILADWLGIEYRTIDISGIVSAFMASIPESESSDRLTRGNLKARTRMSLLYFHANRLNRMVVGTGNKTEILLGYYTKYGDGGVDLEPIGGIYKTEVWELSRRLGIPDPLITKKPSAGLWTGQTDEAELGISYLKVDDVLRMIEEGAEQEKILKDTGISIEQLNSVTRRIERNEHKRKSPPVPELY | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 28295
Sequence Length: 256
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
EC: 6.3.1.5
|
A7IAS7 | MAQELGCRMGQVEQMIRYAYWNSKSQGIVVGVSGGVDSALAAAFCCRAIGPEKVLGLSLPASVSNPQDLSDAQELCAMLGMEHRVVLIDPMLAAFKTIPGFVETPYLLGNLMARIRMTVLYYHANRDHRLVCGTSNRSEAMLGYCTKYGDNAADFQPIVHLYKTDVYEMAKEVKIPKAILEKTPSAGLWAGQSDEGEIGLSYAEIDAALKNLEANGWKAGTPSEEKVLSRAQANAHKRLAAPNLLSVP | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 26893
Sequence Length: 248
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
EC: 6.3.1.5
|
Q12V31 | MDIIQAKDIIIDFIGTKLEGTGIEGAVVGISGGIDSALVAYLSVEALGAENVLGIHMPEASTPKSEIEDASKVAEALGIDFKVINITNVLEVYRTAMPDIDGASAHVDGNLKARIRMSMLYYYANMFGRVVMGTGNKSEILLGYFTKYGDGGVDIEPIGDLYKTEVREMSKMLGVPESILEKAPSAGLWEGQTDEDDLGVTYETIDKVLQPILAGEGQERVHLKLGVPMEEISSILLRVRSNLHKRTTPQIAYLDDLRGDWLS | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 28578
Sequence Length: 263
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
EC: 6.3.1.5
|
Q58747 | MLWGESMEEIVNKITKFIREKVEEANANGVVVGLSGGIDSSVTAYLCVKALGKDKVLGLIMPEKNTNPKDVEHAKMVAENLGIKYIISDITDILKAFGAGGYVPTREFDKIADGNLKARIRMCILYYFANKYNLLVAGTSNKSEIYVGYGTKHGDIACDIRPIGNLFKTEVKKLAKYIGVPKEIIEKPPSAGLWEGQTDEEELDIKYETLDTILKLYEKGKTPEEIHKETNIPLETINYVFDLIKKNEHKRTLPPTPEI | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 28982
Sequence Length: 259
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
EC: 6.3.1.5
|
Q8TVH1 | MAKYEPVIPELEVNPEGEVSKIAEFLRGKFEEAGREIAVVGLSGGVDSSTTLGLAVEALGRENVVALILPERDTPEEDVEDAVEAAERFGVEYHVHDITEVLRAFGTGSYVPCHPFSRKSDANLKPRVRMCVLYYFANELDGLVLGTGNRTEWLTGYFTLHGDGACDVAPIRHLYKTQVYVIAEHLGVPERIVEEKEPSARLWPGQTDEGELGIDYPTLDALLYALVDEGLGPRKAVDWLGERGVEATEEDAEKVLDLVRSSSFKRRPAPGLDLPEPEDPAMSG | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 31191
Sequence Length: 284
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
EC: 6.3.1.5
|
O27554 | MKCVPGLCSEVVSVIEDFIRQKVAESGASGVVLGLSGGVDSSTVAYLAVNALGPDRVLGLIMPSSTTPRDDLRHARTVADELGIESETIDIDPIIESLTGLCSHNANELALANLKPRARMVILYYHANSLNRLVAGTGNRTELLLGYFTKYGDGGVDMLPIGGLYKGQVRELAGRLGVPPEIIKKPPTAGLWHGQTDEEELGMKYDLLDELLCLLVDRKLPVEEVASTLSLPPSEVERIASMVKGSEHKLKPPEVPDIWEVMECSH | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 28722
Sequence Length: 266
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
EC: 6.3.1.5
|
P0A5L7 | MNFYSAYQHGFVRVAACTHHTTIGDPAANAASVLDMARACHDDGAALAVFPELTLSGYSIEDVLLQDSLLDAVEDALLDLVTESADLLPVLVVGAPLRHRHRIYNTAVVIHRGAVLGVVPKSYLPTYREFYERRQMAPGDGERGTIRIGGADVAFGTDLLFAASDLPGFVLHVEICEDMFVPMPPSAEAALAGATVLANLSGSPITIGRAEDRRLLARSASARCLAAYVYAAAGEGESTTDLAWDGQTMIWENGALLAESERFPKGVRRSVADVDTELLRSERLRMGTFDDNRRHHRELTESFRRIDFALDPPAGDIGLLREVERFPFVPADPQRLQQDCYEAYNIQVSGLEQRLRALDYPKVVIGVSGGLDSTHALIVATHAMDREGRPRSDILAFALPGFATGEHTKNNAIKLARALGVTFSEIDIGDTARLMLHTIGHPYSVGEKVYDVTFENVQAGLRTDYLFRIANQRGGIVLGTGDLSELALGWSTYGVGDQMSHYNVNAGVPKTLIQHLIRWVISAGEFGEKVGEVLQSVLDTEITPELIPTGEEELQSSEAKVGPFALQDFSLFQVLRYGFRPSKIAFLAWHAWNDAERGNWPPGFPKSERPSYSLAEIRHWLQIFVQRFYSFSQFKRSALPNGPKVSHGGALSPRGDWRAPSDMSARIWLDQIDREVPKG | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) + L-glutamate + NAD(+)
Sequence Mass (Da): 74683
Sequence Length: 679
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (L-Gln route): step 1/1.
EC: 6.3.5.1
|
P47623 | MTNLIKYLKELQNWLFDYVKKSKAKGVIFGLSGGIDSAVVAAIAKETFGFENHLALIMHINNSKLDFQATSELVKKMQFNSINIELEESFNLLVKTLGIDPKKDFLTAGNIKARLRMITLYAYAQKHNFLVLGTGNFVEYTLGYFTKWGDGACDIAPLAWLLKEDVYKLAKHFNIPEIVITRAPTASLFEGQTDETEMGITYKELDQYLKGDLILSSEKQKIVLDLKAKAEHKHNSPLKFKHLYNFQN | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 28190
Sequence Length: 248
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
EC: 6.3.1.5
|
Q9CBZ6 | MDFYNSYSQGFVRVAACTHHASIGDPTTNAASVLRLARQCHDDGVAVAVFPELTLSGYSIEDILLQDLLLEAVEDTVLDIVVASADLLPVLVIGAPLRYRHRIYNTAVIIHRGVVLGVAPKSYLPTYREFYERRQLAPGDDEHGTIGIGDLRAPFGPDLLFAAADLLGLVLHVEICEDMFVPVPPSAEAALAGATVLANLSGSPITIGRAEDRRLLARSASLRCLAAYVYAAAGEGESTTDLAWDGQTMIWENGVLLAESERFPKGEHRSVADVDTELLRSERLRMGTFNDNRRRHRALVEPFRRIEFRLEPPVGNIGLLREVERFPFVPADPQRLQQDCYEAYNIQVSGLEQRLRALDYPKVVIGVSGGLDSTHALIVAARAMDREGRPRSDILAFTLPGFVTGDRTKSNATELCRALGVTFTEIDIRDTATLMLKKIGHPFSRGEVSYDVTFENVQAGVRTDYLFRLANQHGGIVLGTGDLSELGLGWSTYGVGDQMSHYNINAGVPKTLVQHLIRWVIASSQFEEQVDKVLQSVLDTEITPELIPSDGEEKLQSTEAKVGPFALQDFSLFQVLRYGFRPSKIAFLTWHAWSDPNCGKWPPGFPEDKRLSYSLKEIRHWLQIFVQRFYSFSQFKRSALPNGPKVSHGGALSPRGDWRAPSDMSARIWLDEIEREVPEE | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) + L-glutamate + NAD(+)
Sequence Mass (Da): 75543
Sequence Length: 680
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (L-Gln route): step 1/1.
EC: 6.3.5.1
|
Q98PU6 | MKSNTEIYKNLKLLEDYGTYLIEWIKLKVQQANKKGVIVGISGGIDSALVACLAKKAFPENSLGITMPIGNSMKLDFDDIAKLQKLTKLEIINIDLTLSYDALAKTLDVKNKLAKANIKPRLRMASLYAMAQEKDYLVLGTDNLDEWYLGYFTKYGDGGVDLLPISYLTKSEVISLAQIYKVDKGIIEKKPSAGLWENQEDEKELGYSYSEVDLFLRKKQIDSQIATKIEKQHQMTEHKRQLASKPMDIVDFENKER | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 29182
Sequence Length: 257
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
EC: 6.3.1.5
|
Q5YRN0 | MASLREQIITELGVQPVIEPKTEVRRRVDFLKDYLRSTPAQGFVLGISGGQDSTLTGRLCQLAAEEVRAEGGEATFVAVRLPYGVQADEHDAAVAMEFIGPDRAVTVNVKPGVDATAGAVAEGLGLDALRDFVRGNIKARERMIIQYAIAGQENLLVVGTDHAAEAVTGFFTKYGDGGVDLTPLTGLTKRQGAALLQELGAPPSTWSKVPTADLEDDRPALPDEEALGLRYSEIDDYLEGKEVTEAVAARVEQLYTATRHKRTVPVSPLDSWWR | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 29601
Sequence Length: 274
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
EC: 6.3.1.5
|
A2YII8 | MRLLRVATCNLNQWAMDFDTNLRNVKESIARAKAAGAAVRVGPELELTGYGCEDHFLEQDTAAHAWECLKDILSGGYTDGILCSIGMPVIFKSVRYNCQVFCLNSKIVMIRPKISLANDGNYREFRWFSAWTFKDALVDFQLPLDISEVTSQDTVPFGYGFIQFLDVSLASETCEELFTANAPRIDLALNGVEVFVNASGSHHQLRKLSLRIDSMRNATLACGGVYMYANQQGCDGGRLYYDGCCCIAVNGDVVAQGSQFSLKDVEVLDALVDLDAVSSYRASVSSFREQASHRTKVPFVKVPYKLCKPFQSGMVPTGPVEVMYHRPEEEIAFGPSCWLWDYLRRSRASGFLLPLSGGADSSSVAAIVGCMCQLVVKDIENGDEQVKADAMRIGQYKDGEFPKDSRELAKRLFYTVYMGTENSSEGTRSRAKMLAEEIGSFHLDVPIDSIVSALLSLFERLTGKRPRYKVDGGSNTENLGLQNIQARIRMVLAFMMASLMPWVHNKSGFYLVLGSSNVDEGLRGYLTKYDCSSADINPIGSVSKQDLRAFLRWAAVHLHYSSLAEVEAAPPTAELEPIRADYNQLDEVDMGMTYEELSIYGRLRKIFRCGPVSMFQNLCHRWCGTLSPSEVADKVKHFFKYYAINRHKMTVLTPSYHAESYSPEDNRFDLRQFLYNARWPYQFRKIDELVQDMDKDGKWVNSTEGELRRRKGVRSAEGGGMGVVAVGSANPSAGS | Catalytic Activity: ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) + L-glutamate + NAD(+)
Sequence Mass (Da): 82077
Sequence Length: 735
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (L-Gln route): step 1/1.
EC: 6.3.5.1
|
Q7MAJ5 | MTLTNPSALVNQLVDFLRQELAQRGFKKVVVGLSGGVDSAVVARLCQEAIGENLHALLMPSSVSSKESVEHALLLCERFNLSHHIQSIAPLELAFRELHPEATPLRIGNACARFRMITLYDFSFKENRLVIGTGNKSEILLGYGTLYGDTACALNPIGDLYKTEIFQLAKFLSIPDEIIQKAPSADLFEGQSDEKELGFSYNDMDQLLFDHIELKLSKEELLAKGHAKELVEMVLKRISTNKFKSEMPPIAQVRGRL | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 28616
Sequence Length: 257
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
EC: 6.3.1.5
|
Q9PC24 | MSEFLRIAMAQFDFPVGAVAQNAERIIALIEQARDEHGADVVMFPELALSGYPPEDLLLRPGFLAHCQVAIERIAAATHGIVAVVGWPQSAGSVVYNVASVLCDGQVEQTYRKRELPNYAVFDERRYFEVDPNGSRCVFKVKGVPVGVLICEDLWFSEPLADTVCGGAELVLVPNASPYERGKHAQRDALLAERARETGAAIAYLNVVGGQDALVFDGASVVVDGHGRVHPAAAAFSDQWLVVDYMRSERRFVPLQWVAESEVSINALVWRAVVRGVQDYCRKNGFSKVWVGLSGGIDSALVLAIAVDALGADQVTAVRLPSRYTAELSNDLAAEQCHSLGVRLETVAIEPVFEGLLAALGPLFAGMAPDATEENLQSRSRGVILMALANKFGGLLLTTGNKSEYAVGYATIYGDMCGGYAPLKDIYKSQVFELAQWRNTVSDVLAIPPGVIHRPPSAELRAQQTDQDSLPPYEVLDGILSLYVDQEQSREDIIAAGYAAGVVDYVLNLVKINEWKRHQAAPGPKVSQRAFGRERRYPISNAYRG | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) + L-glutamate + NAD(+)
Sequence Mass (Da): 59261
Sequence Length: 545
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (L-Gln route): step 1/1.
EC: 6.3.5.1
|
P38795 | MSHLITLATCNLNQWALDFEGNRDRILQSIKIAKERGARLRVGPELEITGYGCLDHFLENDVCLHSWEMYAQIIKNKETHGLILDIGMPVLHKNVRYNCRLLSLDGEILFIRPKIWLANDGNYREMRFFTPWMKPGVVEDFILPPEIQKVTGQRLVPFGDAVINSLDTCIGTETCEELFTPQSPHIAMSLDGVEIMTNSSGSHHELRKLNKRLDLILNATKRCGGVYLYANQRGCDGDRLYYDGCALIAINGTIVAQGSQFSLDDVEVVTATVDLEEVRSYRAAVMSRGLQASLAEIKFKRIDIPVELALMTSRFDPTVCPTKVREPFYHSPEEEIALGPACWMWDYLRRCNGTGFFLPLSGGIDSCATAMIVHSMCRLVTDAAQNGNEQVIKDVRKITRSGDDWIPDSPQDLASKIFHSCFMGTENSSKETRNRAKDLSNAIGSYHVDLKMDSLVSSVVSLFEVATGKKPIYKIFGGSQIENLALQNIQARLRMVLSYLFAQLLPWVRGIPNSGGLLVLGSANVDECLRGYLTKYDCSSADINPIGGISKTDLKRFIAYASKQYNMPILNDFLNATPTAELEPMTKDYVQSDEIDMGMTYEELGVFGYLRKVEKCGPYSMFLKLLHQWSPKLTPRQISEKVKRFFFFYAINRHKQTVLTPSYHAEQYSPEDNRFDLRPFLINPRFPWASRKIDEVVEQCEAHKGSTLDIMSID | Catalytic Activity: ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) + L-glutamate + NAD(+)
Sequence Mass (Da): 80686
Sequence Length: 714
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (L-Gln route): step 1/1.
EC: 6.3.5.1
|
Q500Y9 | MAIRKLLLLLKPIDPYPFLQTEGASLIKNPQVLQYLESRCKVHKNAIKFCQEILSKKPVEWKPISRNDLSHPIRDVDMVITVGGDGTLLHASHFIDDSVPVLGVNSDPTQAHEVEELSDQFDASRSTGHLCAATVENFEQVLDDILFGRVVPAKVSRISLKLNSETLLSHALNDILIAQPCPAAVSRFSFKIKNKDGASSPKTVNCRSSGLRICTAAGSTAAMQSAGGFVMPMLSRDLQFMVREPISPGSTASLMHSTFKPDQFMDVNWYSDHGTIYIDGCQVQHSVQLGDTIEISSDAPVLNVFLSHGISQIRSRY | Function: Phosphorylates specifically NADH. Can phosphorylate NAD with a 100-fold decrease in efficiency compared to NADH. Prefers ATP as nucleoside triphosphate substrate. Can also utilize UTP, GTP and CTP. Key source of the cellular reductant NADPH which is an important antioxidant factor.
Catalytic Activity: ATP + NADH = ADP + H(+) + NADPH
Sequence Mass (Da): 34831
Sequence Length: 317
Subcellular Location: Cytoplasm
EC: 2.7.1.86
|
Q6EQG2 | MALRRVLLFVKPFDVYPPRPLAAAASSPPPPPPPLRVSNPKVLNYLDDRCRVHKETINLCKSVLQRKSIDWISVQRNDMSNPIHDVDLVISVGGDGTLLRASHFLNSSIPVLGVNSDPTCPDEVDELTDEFDARRSTGHLCAATAANFEQILDATLDGSRQPSELSRISVKLNGLQLPTYALNDILVSHPCPASVSRFSFRKRSNTGESSHLINCRSSGLRVATPAGSTAAMLSAGGFVMPISSHELQYMIREPISPRDADKPLLHGLVKQGQHILVVWYNEEGAVYFDGSHVMHSIQHGDTLEISSDAPILKVILPENLLKQGS | Function: Key source of the cellular reductant NADPH which is an important antioxidant factor.
Catalytic Activity: ATP + NADH = ADP + H(+) + NADPH
Sequence Mass (Da): 35517
Sequence Length: 325
Subcellular Location: Cytoplasm
EC: 2.7.1.86
|
Q56YN3 | MSSTYKLNHTDSFANGDAKSLLPNPENGFTHLTSLAQSEKAVQELLLQQTPMQATDDHLVEFSEALRTVAKALRGAAEGKALAQAEAAEWKRRYELERSKNVELQHKELSNGVCADESNGQRMEHLAKSPRLYAQEISSNGMETICSHEVLQDGGFNSFNNKLKRKASFKLSWGCKGMANDQHKKEIVSFERGNISTAERSSKQISLTWESDPQTVLIITKPNSTSVRVLSVDMVRWLRTQKGLNIYVEPRVKEELLSESSSFNFVQTWEDDKEISLLHTKVDLLITLGGDGTVLWAASMFKGPVPPIVPFSMGSLGFMTPFHSEQYRDCLEAILKGPISITLRHRLQCHIIRDKATHEYEPEETMLVLNEVTIDRGISSYLTNLECYCDNSFVTCVQGDGLILSTTSGSTAYSLAAGGSMVHPQVPGILFTPICPHSLSFRPLILPEHVTVRVQVPFNSRSSAWVSFDGKDRKQLEAGDALVCSMAPWPVSTACQVESTNDFLRSIHDGLHWNLRKTQSADGP | Function: Phosphorylates both NAD(+) and NADH, with a twofold preference for NADH. Source of the cellular reductant NADPH which is an important antioxidant factor.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 58245
Sequence Length: 524
EC: 2.7.1.23
|
A7ZQ55 | MNNHFKCIGIVGHPRHPTALTTHEMLYRWLCTKGYEVIVEQQIAHELQLKNVKTGTLAEIGQLADLAVVVGGDGNMLGAARTLARYDIKVIGINRGNLGFLTDLDPDNAQQQLADVLEGHYISEKRFLLEAQVCQQDCQKRISTAINEVVLHPGKVAHMIEFEVYIDEIFAFSQRSDGLIISTPTGSTAYSLSAGGPILTPSLDAITLVPMFPHTLSARPLVINSSSTIRLRFSHRRNDLEISCDSQIALPIQEGEDVLIRRCDYHLNLIHPKDYSYFNTLSTKLGWSKKLF | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 32566
Sequence Length: 292
Subcellular Location: Cytoplasm
EC: 2.7.1.23
|
Q8EGS1 | MTTKFHTIGLIGKPHHPGTNQTLKRLHHWLTMQGYEVLVEERVATELGPHIVAVDLLEIGERCDLAIVVGGDGNMLGAARVLARFEVGVIGVNRGNLGFLTDLPPDAFEEALAKVLDGEFDTEHRFLLEAEVYRHGQLKASNTAVNEAVLHPGKIAHMIEFEVYIDNQFMYSQRADGMIVSTPTGSTAYALSAGGAILTPNLQALILVPMFPHTLSCRPIVVDACSTIKMVVSPENGENLEVSCDGHVHLAVLPGDEIIVRRSSEQLRLIHPKGHNYFHVLRSKLGWGSKLF | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 32019
Sequence Length: 292
Subcellular Location: Cytoplasm
EC: 2.7.1.23
|
Q02A16 | MPIIKTAGIISKPNSTAAEEIVPKLIEWLRRRGIAVRIDEQTSLYSGGVSGMPREEVPQSCDLVVVLGGDGTLLSAARAIGRREIPLFPVNLGGLGFLTAISIEELYPELERALRGEHRIAKRKLMTTEVIRENNVIASFDALNDAVLTKSSIARMIDLDTYVDEQFVCAYKADGLIIATPTGSTAYSLSAGGPIIFPSVPAICLTPICPHMLTNRPVLVPETSVIRVASRGPDESVYLTIDGQVGTPIREHDTVVCHSSHHSLLLIRPPRMMFFDVLRQKLKWGER | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 31420
Sequence Length: 287
Subcellular Location: Cytoplasm
EC: 2.7.1.23
|
P34480 | MLPRKLKIDSTELAEITNELVQFLNCLVLRSGGLKKEHIWVRNGRILDERTVFFEEKTMADVQIDCEGLILSPGFIDLQLNGGFGIDFSTYNSDDKEYQEGLALVAKQLLAHGVTSFSPTVITSSPETYHKILPLLKPSNASSEGAGNLGAHLEGPFISADKRGCHPEQLVITSLSPNPVEIIEHVYGSTENIAIVTMAPELEGAQEAIEYFVSTGTTVSVGHSSAKLGPGEMAVLSGAKMITHLFNAMQSYHHRDPGLIGLLTSSKLTPDHPLYYGIISDGIHTHDSALRIAYHTNSAGLVLVTDAIAALGMSDGVHKLGTQTIHVKGLEAKLDGTNTTAGSVASMPYCIRHLMKATGCPIEFALQSATHKPATLLGVSDEKGTLDVGRLADFVLIDKNVTVKATFCSGKRVFLAQD | Cofactor: Binds 1 divalent metal cation per subunit.
Catalytic Activity: H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-glucosamine 6-phosphate
Sequence Mass (Da): 44887
Sequence Length: 418
EC: 3.5.1.25
|
Q6P0U0 | MPSNKSVSDAPITQFVNCRILKNHKLQWEDLWVREGKILNPEKLFFDEQGFADHRVDCENKIIAPGFIDVQLNGGYGIDFSQASSDIRGGVALVAKKILEHGVTSFCPTLVTSPPHIYHKVIPELRVQDGGPEGAGVLGIHLEGPFISEEKRGAHPPKFLRTFQSGGVADLMETYGQLENVAMVTLAPELTNSAAAIHELSSRGITVSVGHSMADLSQAEEAVQNGATFITHLFNAMLPFHHRDPGIVGLLTSDRIPPGRTVYYGMIADGIHTHPAALRIAHRAHPAGLVLVTDAVTAMGLPPGRHTLGQQQIDIQGLHAYVAGTTTLSGSIATMDMCVRHFREASGCTVEAALEAASLHPAQLLGISHRKGTLEFGADADFIVLDDMLTVRETYIAGQQVWRK | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Hydrolyzes the N-glycolyl group from N-glycolylglucosamine 6-phosphate (GlcNGc-6-P) in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway.
Catalytic Activity: H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-glucosamine 6-phosphate
Sequence Mass (Da): 43686
Sequence Length: 404
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation.
EC: 3.5.1.25
|
Q9VR81 | MDVRIKCNSEEPESPEQKILASSQRLLQFTNCRLVRDHRIIHDDLWVRDGRIVNPEPVFFDERTKAHCRIDCGGAIIAPGYIDLQINGGYGVDFSYDTETIEEGVATVARGLVKSGVTSFCPTLVTSPSDSYHTILPRIPAEVPKGAGILGIHAEGPFINPQKKGAHPEHCIQTIDKGLSTLKETYGSLERIKIITLAPEKVTDPEVIGQLVERGITVALGHSMASLSDGERAVQQGATLITHLFNAMLPFHHRDPGLVGLLASDAVPHGRTVYFGIISDGVHTHPAALRIAYRTHPQGLILVTDAISALGLEEGVHHIGQLPLQVKQGKAFIAGTETLCGSIAPMDECVRIFQKATDCSVVYAIEAATLHPAQCLKIEKQKGTLDFGSDADFVLLDDQLRVLSTWIAGVCVHRTVK | Cofactor: Binds 1 divalent metal cation per subunit.
Catalytic Activity: H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-glucosamine 6-phosphate
Sequence Mass (Da): 45283
Sequence Length: 417
EC: 3.5.1.25
|
P0AF19 | MYALTQGRIFTGHEFLDDHAVVIADGLIKSVCPVAELPPEIEQRSLNGAILSPGFIDVQLNGCGGVQFNDTAEAVSVETLEIMQKANEKSGCTNYLPTLITTSDELMKQGVRVMREYLAKHPNQALGLHLEGPWLNLVKKGTHNPNFVRKPDAALVDFLCENADVITKVTLAPEMVPAEVISKLANAGIVVSAGHSNATLKEAKAGFRAGITFATHLYNAMPYITGREPGLAGAILDEADIYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEGVRNLVEHCGIALDEVLRMATLYPARAIGVEKRLGTLAAGKVANLTAFTPDFKITKTIVNGNEVVTQ | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the first committed step in the biosynthesis of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-phosphate and acetate. Can probably also catalyze the deacetylation of N-acetyl-D-galactosamine 6-phosphate to D-galactosamine 6-phosphate (Probable).
Catalytic Activity: H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-glucosamine 6-phosphate
Sequence Mass (Da): 40949
Sequence Length: 382
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 4/5.
EC: 3.5.1.25
|
P44537 | MKYALINCVIYTKYDVLRDFAVIINGEIIEAVIPQAELETGIKTIDLQGNNLTAGFIDLQLNGCGGVMFNDQTSVETLEIMQETNLKSGCTSFLPTFITAPDENIKSAVKIMREYLNKHKNQALGLHIEGPYLSIEKKGVHRPEYIREITPEMKDFLCENGDVITKMTIAAENPTINYTPDFVKAGIIVSVGHSNATYEVAKAAFHKGATFATHLHNAMSPISSGREMGVVGAVLDSDVYTGIIVDGVHINYGNVRIDKKIKGDKLCIVTDSIAAAGAPPELESFTFVGKTIYIKEGRCYDANDTIAGASITMMESIKNAVEYVEIPLAEAIRMSNLYPARAIGIDDRLGSVEKGKIANLAVFTPNYQVIGTVVNGKWKEN | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the first committed step in the biosynthesis of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-phosphate and acetate.
Catalytic Activity: H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-glucosamine 6-phosphate
Sequence Mass (Da): 41593
Sequence Length: 381
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 4/5.
EC: 3.5.1.25
|
Q9Y303 | MRGEQGAAGARVLQFTNCRILRGGKLLREDLWVRGGRILDPEKLFFEERRVADERRDCGGRILAPGFIDVQINGGFGVDFSQATEDVGSGVALVARRILSHGVTSFCPTLVTSPPEVYHKVVPQIPVKSGGPHGAGVLGLHLEGPFISREKRGAHPEAHLRSFEADAFQDLLATYGPLDNVRIVTLAPELGRSHEVIRALTARGICVSLGHSVADLRAAEDAVWSGATFITHLFNAMLPFHHRDPGIVGLLTSDRLPAGRCIFYGMIADGTHTNPAALRIAHRAHPQGLVLVTDAIPALGLGNGRHTLGQQEVEVDGLTAYVAGTKTLSGSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGADADFVVLDDSLHVQATYISGELVWQADAARQ | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Hydrolyzes the N-glycolyl group from N-glycolylglucosamine 6-phosphate (GlcNGc-6-P) in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. Although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded.
Catalytic Activity: H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-glucosamine 6-phosphate
Sequence Mass (Da): 43748
Sequence Length: 409
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation.
EC: 3.5.1.25
|
Q84F86 | MFFLSLIIRNITVVNASGRDEQMDVWMKDGKIAQIAQHIHAQGVDQLEGSGKFLLPGFIDMHIHGSAQMDTMDASDEGLHIHGPITIKEGTTSFLATTMTQSFDWFDRAQRQCGNNFSPKSDEAEVLGLHIEGPFVSKQRAGAQPLDYIVQPDMEVIKKWQALSGQKIKQITLAPEEPNGMAAVQSLSESGVIVSIGHSDATFEQMQEAVQLGASQGTHLYNQMRPFHHRDPGVVGGVLLVDAIKAELIVDFIHMHEGAVEMAYRLKGADGIILITDAMRAKGMPYGEYDLGGQLVHVTESGAHLSNGSLAGSILTMDQAVRNMRQITNCTLEELVKMSSYNAAQQLKLTNKGQLTEGYDADAVIVDEHLLLHQTIKAGRIRVQTNN | Cofactor: Binds 2 divalent metal cations per subunit.
Function: Involved in the first committed step in the biosynthesis of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-phosphate and acetate.
Catalytic Activity: H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-glucosamine 6-phosphate
Sequence Mass (Da): 42382
Sequence Length: 387
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 4/5.
EC: 3.5.1.25
|
Q8JZV7 | MRSGQCAAGAPVLQFTNCRILRGGTLLREDLWVRGGRILDPEKLFFEERRVADEQRDCGGRILAPGFIDVQINGGFGVDFSKATEDVGSGVALVARRLLSHGVTSFCPTLVTSPPEVYHKVLPQIPVKSGGPHGAGVLGVHLEGPFISREKRGAHPEAYLRSFEANAFHDVLATYGPLDNVCIVTLAPELDRSHEVIQALTAQGIRVSLGHSVADLRAAEVAVQSGATFITHLFNAMLPFHHRDPGIVGLLTSDQLPPGHCIFYGMIADGIHTNPAALRIAHRAHPQGLVLVTDAVPALGLGNGRHTLGQQEVEVDGLIAYIAGTKTLGGSIAPMDVCVRHFLQATGCSVESALEAASLHPAQMLGLEKTKGSLDFGADADFVVLDDTLHVQATYISGELVWQAEEAGP | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Hydrolyzes the N-glycolyl group from N-glycolylglucosamine 6-phosphate (GlcNGc-6-P) in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway.
Catalytic Activity: H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-glucosamine 6-phosphate
Sequence Mass (Da): 43501
Sequence Length: 409
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation.
EC: 3.5.1.25
|
O32445 | MYALTNCKIYTGNDVLVKHAVIINGDKIEAVCPIESLPSEMNVVDLNGANLSPGFIDLQLNGCGGVMFNDEITAETIDTMHKANLKSGCTSFLPTLITSSDENMRQAIAAAREYQAKYPNQSLGLHLEGPYLNVMKKGIHSVDFIRPSDDTMIDTICANSDVIAKVTLAPENNKPEHIEKLVKAGIVVSIGHTNATYSEARKSFESGITFATHLFNAMTPMVGREPGVVGAIYDTPEVYAGIIADGFHVDYANIRIAHKIKGEKLVLVTDATAPAGAEMDYFIFVGKKVYYRDGKCVDENGTLGGSALTMIEAVQNTVEHVGIALDEALRMATLYPAKAIGVDEKLGRIKKGMIANLTVFDRDFNVKATVVNGQYEQN | Cofactor: Binds 1 divalent metal cation per subunit. Ni(2+) ion is seen in the structure.
Function: Involved in the first committed step in the biosynthesis of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-phosphate and acetate.
Catalytic Activity: H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-glucosamine 6-phosphate
Sequence Mass (Da): 40956
Sequence Length: 378
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 4/5.
EC: 3.5.1.25
|
P96166 | MESKSHAHCFRAQRVLHGKQWQQDAVVTVDENGTISAIESYDGQRHADAIPLGPVDLMPGLIDSHVHGSQGCDVMDATHDSLNTMSRYFATLGVTAFVATTVTAPVAKIRAALAQVAKSKHDGVDGAEILGAYLEGPYFTEKNKGAHPTQWFRELAVEELEDWISYSDNQLLKVALAPEKTGALDAIRYLDAHGIHVMLGHSDADYEQVKAALAAGAKGIVHCYNGMRGLHHRDPGVVGAGLLHPHCFVEMIADGHHVHPAAIDVAHRCCGSRMTLITDAMRATGMPDGQYTLGEYQVDMKQGVVMTSSGGLAGSTLTLLRGVKNIHRWLNVPIEQAWLMASYTPAESLGIQHQLGSLEVGKYASMVAVSSDFSIEKTWVKGRLVFDAATSPRQEALCI | Cofactor: Binds 2 divalent metal cations per subunit.
Function: Involved in the first committed step in the biosynthesis of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-phosphate and acetate.
Catalytic Activity: H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-glucosamine 6-phosphate
Sequence Mass (Da): 43122
Sequence Length: 399
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 4/5.
EC: 3.5.1.25
|
A9NEX8 | MKINVFETKEELYRAVADFYIKAINEKPNMTLGLATGTTPIPLYQNLIKAYQDKLVSFKDITTFNLDEYIGLPKTHKESYFSFMRNQLFNHVDINLDNTHIPSGVLEPSEAIKEFQTALDAHQIDIQLLGLGSNGHIGFNEPGTSFESTTHKTQLALSTIQDNSRMFDSIDEVPTESITMGIKDIMRASKIVMIATGAQKADAVYKMIQGPVDESLPASILQKHDDVVIFLDKDAASLLK | Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Catalytic Activity: alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+)
Sequence Mass (Da): 26786
Sequence Length: 240
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 5/5.
EC: 3.5.99.6
|
Q8CTR3 | MKIINLDSKNLASFYVACELFKQIQQHPHAKLGLATGGTMTDVYHYLVNLLIKNKVDVSQVETFNLDEYVGLKASHQQSYHTYMNKVLFEQYPHFVKNHIHIPDGLSENLEAEAERYNNLLDERGPIDIQILGIGENGHIGFNEPGTDFNSETHVVNLTESTIKANSRFFDNEKDVPRQAVSMGVKSILKAKRIILLAFGPKKKEAISKLLNEQVTEDVPATILHTHPNVEVYVDDEAAPDCL | Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Catalytic Activity: alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+)
Sequence Mass (Da): 27383
Sequence Length: 243
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 5/5.
EC: 3.5.99.6
|
Q9K487 | MEVVIVPDAKAGGELIAEAMAQLLRRKPDALLGVATGSTPLPVYEALAAKVRSGAVDTAQARIAQLDEYVGLPAEHPESYRSVLRREVLEPLGIDMDAFMGPDGTAADVQAACEAYDTALGGSGGVDLQLLGIGTDGHIGFNEPCSSLASRTRIKTLTEQTRIDNARFFDGDIEQVPHHVITQGIGTILEARHVVLLATGEGKADAVAASVEGPVAAVCPASALQLHPHATVVVDEAAASKLKLADYFRHTYAHKPDWQGI | Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Catalytic Activity: alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+)
Sequence Mass (Da): 27446
Sequence Length: 261
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 5/5.
EC: 3.5.99.6
|
Q8DV70 | MKTIKVKNKTEGSKVAFRMLEEEITFGAKTLGLATGSTPLELYKEIRESHLDFSDMVSINLDEYVGLSADDKQSYAYFMKQNLFAAKPFKKSYLPNGLAADLAKETEYYDQILAQYPIDLQILGIGRNAHIGFNEPGTAFSSQTHLVDLTPSTIAANSRFFEKAEDVPKQAISMGLASIMSAKMILLMAFGEEKAEAVAAMVKGPVTEEIPASILQTHPKVILIVDEKAGAGI | Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Catalytic Activity: alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+)
Sequence Mass (Da): 25473
Sequence Length: 233
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 5/5.
EC: 3.5.99.6
|
Q5XBG4 | MKIIRVQDQIEGGKIAFTLLKDSLAKGAKTLGLATGSSPISFYQEMVKSRLDFSDLTSINLDEYVGLSVESDQSYDYFMRQNLFNAKPFKKNYLPNGLATDVEAEAKRYDQIIAEHPIDFQVLGIGRNGHIGFNEPGTSFEEETHVVDLQESTIEANSRFFTSIDDVPKQAISMGIASIMKSKMIVLLAFGQEKADAIKGMVFGPITEDLPASILQKHDHVIVIVDEAAASQLD | Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Catalytic Activity: alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+)
Sequence Mass (Da): 25823
Sequence Length: 234
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 5/5.
EC: 3.5.99.6
|
Q9UK23 | MATSTGRWLLLRLALFGFLWEASGGLDSGASRDDDLLLPYPRARARLPRDCTRVRAGNREHESWPPPPATPGAGGLAVRTFVSHFRDRAVAGHLTRAVEPLRTFSVLEPGGPGGCAARRRATVEETARAADCRVAQNGGFFRMNSGECLGNVVSDERRVSSSGGLQNAQFGIRRDGTLVTGYLSEEEVLDTENPFVQLLSGVVWLIRNGSIYINESQATECDETQETGSFSKFVNVISARTAIGHDRKGQLVLFHADGQTEQRGINLWEMAEFLLKQDVVNAINLDGGGSATFVLNGTLASYPSDHCQDNMWRCPRQVSTVVCVHEPRCQPPDCHGHGTCVDGHCQCTGHFWRGPGCDELDCGPSNCSQHGLCTETGCRCDAGWTGSNCSEECPLGWHGPGCQRPCKCEHHCPCDPKTGNCSVSRVKQCLQPPEATLRAGELSFFTRTAWLALTLALAFLLLISTAANLSLLLSRAERNRRLHGDYAYHPLQEMNGEPLAAEKEQPGGAHNPFKD | Function: Catalyzes the second step in the formation of the mannose 6-phosphate targeting signal on lysosomal enzyme oligosaccharides by removing GlcNAc residues from GlcNAc-alpha-P-mannose moieties, which are formed in the first step. Also hydrolyzes UDP-GlcNAc, a sugar donor for Golgi N-acetylglucosaminyltransferases.
PTM: The precursor is cleaved and activated in the trans-Golgi network by a furin endopeptidase.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: H2O + N(4)-[6-(N-acetyl-alpha-D-glucosaminyl-1-phospho)-alpha-D-mannosyl-(1->2)-alpha-D-mannosyl-(glycan)]-L-asparaginyl-[protein] = H(+) + N(4)-[6-phospho-alpha-D-mannosyl-(1->2)-alpha-D-mannosyl-(glycan)]-L-asparaginyl-[protein] + N-acetyl-D-glucosamine
Sequence Mass (Da): 56073
Sequence Length: 515
Domain: The tyrosine-based internalization signal may be essential for its retrieval from the plasma membrane to the TGN.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus
EC: 3.1.4.45
|
Q8BJ48 | MAAPRGPGLFLIPALLGLLGVAWCSLSFGVSRDDDLLLPYPLARRRPSRDCARVRSGSPEQESWPPPPTNPGASHHAAVRTFVSHFEGRAVAGHLTRVADPLRTFSVLEPGGAGGCAQKRRATVEDTAVPAGCRIAQNGGFFRMSTGECLGNVVSDGRLVSSSGGLQNAQFGIRRDGTIVTGYLSEEEVLDPVNPFVQLLSGVVWLIRNGNIYINESQAIECDETQETGSFSKFVNVMSARTAVGHDREGQLILFHADGQTEQRGLNLWEMAEFLRQQDVVNAINLDGGGSATFVLNGTLASYPSDHCQDNMWRCPRQVSTVVCVHEPRCQPPDCSGHGTCVDGHCECTSHFWRGEACSELDCGPSNCSQHGLCTETGCHCDAGWTGSNCSEECPLGWYGPGCQRPCQCEHQCSCDPQTGNCSISQVRQCLQPTEATPRAGELASFTRTTWLALTLTLIFLLLISTGVNVSLFLGSRAERNRHLDGDYVYHPLQEVNGEALTAEKEHMEETSNPFKD | Function: Catalyzes the second step in the formation of the mannose 6-phosphate targeting signal on lysosomal enzyme oligosaccharides by removing GlcNAc residues from GlcNAc-alpha-P-mannose moieties, which are formed in the first step. Also hydrolyzes UDP-GlcNAc, a sugar donor for Golgi N-acetylglucosaminyltransferases.
PTM: The precursor is cleaved and activated in the trans-Golgi network by a furin endopeptidase.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: H2O + N(4)-[6-(N-acetyl-alpha-D-glucosaminyl-1-phospho)-alpha-D-mannosyl-(1->2)-alpha-D-mannosyl-(glycan)]-L-asparaginyl-[protein] = H(+) + N(4)-[6-phospho-alpha-D-mannosyl-(1->2)-alpha-D-mannosyl-(glycan)]-L-asparaginyl-[protein] + N-acetyl-D-glucosamine
Sequence Mass (Da): 56044
Sequence Length: 517
Domain: The tyrosine-based internalization signal may be essential for its retrieval from the plasma membrane to the TGN.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus
EC: 3.1.4.45
|
Q84JF4 | MTERGAMVVSSSTCYVPFRCPQARKDFAFVEPSKKLNPNRVLIKPPVYTYSPALTAAKCNIFDYAETGENLVGDKQFVRWFREAWPYLWAHRSCTFVVTISGDVLDGPYCDLVLKDIAFLHHLGIKFVLVPGTQVQIDQLLAERGREPTYVGRYRVTDSASLQAAKEAAGAISVMIEAKLSPGPSIYNIRRHGDSSRLHETGVRVDTGNFFAAKRRGVVDGVDFGATGLVKKIDVDRIRERLDSGSVVLLRNLGHSSTGEVLNCNTYEVATACALAIGADKLICIMDGPVLDENGHLVRFLTLQEADTLVRKRAQQSEIAANYVKAVGDGGISSFPEPLGYNGMVTTPNNHIGRPIWEKLSPTFQNGVGFDNGNGLWSGEQGFAIGGEERISRLNGYLSELAAAAFVCRGGVKRVHLLDGTISGVLLLELFKRDGMGTMVASDVYEGNREAKVEDLAGIRQIIKPLEESGALVRRTDEELLRALDSFVVVEREGHIIACAALFPFFEEKCGEVAAIAVASDCRGQGQGDKLLDYIEKKASALGLEMLFLLTTRTADWFVRRGFQECPIEMIPEARRERINLSRRSKYYMKKLLPDRSGISVVRTFQYDS | Function: N-acetylglutamate synthase involved in arginine biosynthesis.
Catalytic Activity: acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate
Sequence Mass (Da): 67179
Sequence Length: 609
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
Subcellular Location: Plastid
EC: 2.3.1.1
|
B5X4Z4 | MERGALVGSSSTSSYYVPYHFRQSKSNFSSFKPKNKLNPTQFRFNCSWFKPVSSITAAKCNMFDYAVTAAGDVEAEHPVDDKQFVRWFREAWPYLWAHRGCTFVVIISGEIIAGSSCDAILKDIAFLHHLGIRFVLVPGTQEQIDQLLAERGREATYVGRYRVTDAASLQAAKEAAGAISVMLEAKLSPGPSICNIRRHGDRSRLHDIGVRVDTGNFFAAKRRGVVDGVDFGATGEVKKIDVDRICERLDGGSVVLLRNLGHSSSGEVLNCNTYEVATACALAIGADKLICIMDGPILDESGHLIHFLTLQEADMLVRKRAQQSDIAANYVKAVGDGSMAYPEPPNNTNGNITSAQNGRAVSFWGNGNHTPIFQNGVGFDNGNGLWPCEQGFAIGGEERLSRLNGYLSELAAAAFVCRGGVKRVHLLDGTISGVLLLELFKRDGMGTMVASDVYEGTRDARVEDLAGIRHIIKPLEESGILVRRTDEELLRALDSFVVVEREGQIIACAALFPFFKDKCGEVAAIAVASDCRGQGQGDKLLDYIEKKASSLGLEKLFLLTTRTADWFVRRGFQECSIEIIPESRRQRINLSRNSKYYMKKLIPDRSGISVMRI | Function: N-acetylglutamate synthase involved in arginine biosynthesis.
Catalytic Activity: acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate
Sequence Mass (Da): 67395
Sequence Length: 613
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
Subcellular Location: Plastid
EC: 2.3.1.1
|
Q75A07 | MLFRRLLTTKVGYHTPNYVNRRLILSVLKSTATRREAKDYLTKYGDPAVAYHCVLYLRGTKTFSAGLINDFAIMLGRLRLLGIRPLVVLSPSKHVMTESEILRETFYKHGLQSIPINEPMASGTRETILQNGASYNSIIPIIMPFVYHQQRAKRMLAEDEVAFMRELVAYMPCRIDKFFIINRYGGIPSSERHDNSHVFVNLSQEYGSLAEVLKQQITDLRHEMDDGLLAERRATDGSYKEFQYTTLTESLTDLELMSAVLSLLLPSSTGLITSMHSAVTNSRYNPLLYNVLTDRSLVSSSLPSFKRDPISDNAWYELPACGAKIGTQRANPIFSTTVLKQGVDIKLYDYSTLTKENSVGFHELLSTAGSAQLPAHKRVNLTKLKGIIEHSFDRNLDMSHYLKRINGKIASIIVIGDYEGIAILTYEGPEKRPFAYLDKFAVLPHLRGSLCISDVIFNLMFKKFGDELVWRSRRENVVNNWYFQRSVGVLDLSIDIGHGPKKDNIFKLFYYGGKKGTQFYDFDRLREYITYVRDIEPSWSRK | Function: N-acetylglutamate synthase involved in arginine biosynthesis.
Catalytic Activity: acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate
Sequence Mass (Da): 61904
Sequence Length: 542
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
Subcellular Location: Mitochondrion
EC: 2.3.1.1
|
A2QGF0 | MSSRTLVGLRSTTSTHLQRSGVAAAAAVSSSSTSSSGSAPRRCLSSASGRQVQQSAEFSSSSKSWDRLGRRAKEKLLDREFFLSLLNSASTKREAKSYLARLKAQHQGTPPLKPAAKQPGVAEAAAPVSSGASSTSFYGASRSVYDSPVFRHDSTPTPPLQDVSERLHLALVKITTPQLLDDSTVNGVAKTLSQLNRLGMACCVVVDPGTAGDSNQLRRIAAEQADRISTAVDAQPDSKSAHIDSVLSVSALNPEAPKVLSRKLLLGPLRDGHIVVLAPIAYTEDVPRAVTVSASDAILALTKELAGLATNPDPDEDPIRTAQRIAGLQEEVSLDRVILLDPLGGIPAFSGPQTSHVFINMEQEFDDIENELLRVWQSAASAKNNLPEEGLPSIADSNPLSKFADTEVVPVPPSQKAYSSDLTLGTSMVEGHINNLRLSQAALAMLPSASSSIITSPLEVANSAQSPGGASPDVSAVGTRRQRNPLIHNLLTDKPLLSSSLPLSRRAALNGRRDSIATQPSHTTFVKRGMPLTIIPNPWLSPWTAKDRPRLGLDDPSIDLPRLVHLIEDSFNRKLDVQDYLNRVNGRLAGLIIAGEYEGGAILTWELPPGVEDDGSEASQARMVPYLDKFAVLKRSQGAGGVADIVFNAMVRSCFPNGVCWRSRKDNPVNKWYFERSQGTWKLSDMNWTMFWTTPGLTEDSQKFRDYEAVCRSIQPSWADDTGVVD | Function: N-acetylglutamate synthase involved in arginine biosynthesis.
Catalytic Activity: acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate
Sequence Mass (Da): 78172
Sequence Length: 726
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
Subcellular Location: Mitochondrion
EC: 2.3.1.1
|
A6SG85 | MLLQNLALKKGKEAAGHNIQSLTKHGNYFVQSSDRRRAYTSNQSAADKVREELAKETCEKLSSQHQAKKKAKAIDRDFFLSVLGSSATKREARSYIQNFKPLNTSPAKPISQEPVHKNTNENGANLGSIYTATRAVAESPKFVQQPAVSQSTLGGSILHVALVKVRAPQLLDDETLNGIGKTLSKLCRLGLISTVVVDCEDGTDTHLKVSECEWRNRIKEQAARVVTAIDASGTEARLVDNVIGIAEDGSDVKQQPYLKGGVHVTFRELLMTPLRRGVLPVLPSIGHTDATQTAVSITASDVVLALTREFAGFRSPQSPDEHPNVVKEHLQALQNEVSLDRLILIDPLGGIPASDRRNGYHVFLNMEQEYEQAKQDLIKTGGLYSETSSRSTRAEADSNFNLRDDIPLSSFTEQKSGELEYSPRHQNDSPTQQDQRMKFHLDNLELVRSALAILPPSSSALVTTPDEAANSGKQHEFKAAGVGTRRQRNPLIHNLLTDKPAFSSSLPAGRLGPLDKNEPITPSTKLAPATFAKHGMPVTIFPDPKTTPWQPPIAGVPQISLTDPQIDLPRLVHLIEDSFNKKLDVQDYLRRVNNRIAGVIIAGEYEGGALLTWELPPGVPDDGSEESRKRMVPYLDKFAVLKRSQGSGGVADVVFKSMVRDCFPGGVCWRSRKDNPVNKWYFERSRATLKLMDTNWTMFFTTPEENMDQQTFQDYEAVCKTIEPSWADKQGVQD | Function: N-acetylglutamate synthase involved in arginine biosynthesis.
Catalytic Activity: acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate
Sequence Mass (Da): 81144
Sequence Length: 734
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
Subcellular Location: Mitochondrion
EC: 2.3.1.1
|
Q59MB6 | MSKLKTLNRQFISNLETHKVTTDAKRNLILSILKSTTTKREAKNYLTKYQNQFDFNDDLDFNKSIKIKNEQSSLTNRDSQRELFINRFLNQSNPFINVYDKEDVKLQKVPLRLAIFKIKFTKITIKQWKGIAETFKRLITLGISPIIMLDYDHLPSDSYKNNELYMINQGNKMLNYLGHPEEESDLKVTLLRSLFTSHKGVPTLDSLESILIPLYQGIIPIIQPIVYNADLSKQEFLASDKLLLGLSSALIEKRTTDLLSIEKIVMIDPIGGIPSIERHQTSHVFINLSQEYSDILSELFIGHIEPKYRDTHVDNLNTMNNVLSYINEKSGNDETTGIITTPEIMSINIDQLNPIIYNVLTDRAIISSSLPSTTNRTPHLSTTIIKKGVEVQIFDVDNYDKDLTMQNLFDDKLVNKEKLIDLLNDSFGKSLDVGPYLDRINKNIATVVIVGDYDGAAIITWEYSKGEKIAYLDKFAIAKKNQGLPGLADVIFKIILQSHPFELIWRSRKNNPVNKWYFERCCGCMSAPDSQWKIFYTGEVFDKKIDRFKRKLRHQNGVVDIDRKLQQYSEICEGITPSFK | Function: N-acetylglutamate synthase involved in arginine biosynthesis.
Catalytic Activity: acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate
Sequence Mass (Da): 66683
Sequence Length: 580
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
Subcellular Location: Mitochondrion
EC: 2.3.1.1
|
Q1DNE1 | MSRSTVLGWCTQSCRLLQKHDHSFSFPTFNGSPPLKKRRFCDSAAPAAPRPSIHRPSEYIPHSKSGGEAPQDLGHKAREKEAEKEFYLSLLCSASTKREAKSYLSRFKAQKTTANDGCQHITPRRGDLISDLELMKDKPGVNLGSMFSETRTVAETPAPKQEWSSAQSTELFREKIHVALVKLRKPQLLDDQTLHGVAKTLVQLSRLGMSCCIVIDVGTDKDETHRRIIAREQADRLSAVIDANHGPDSRQLDSIITVPSATDMKLSVLSRGPLLSPLQQGHVVVVVPVGYANDTQRAVLLPANEVVFALSKELAGLELRSGPDEDATTTANKVNDMQKQVSLDRIIILDPAGGIPSLQRRPHVFINLEQEFEDIARELSLGSQTGFLSINDSGTASHKMPVSSLGKSNPISIFVEEELVSLPKTLGESQEMPRNGKRFAEHLENLNLLQRTLSYLPPSSSGIIVTPHEVALSAKGPLNTSAVSAVRTRRQRNPLIHNLLTDKPFQSASLPLGRLGVKSDCMSAGQSPATHSTFVKRGMPLTMLPDPRVEVWAAKKRGEPALTLDDPRIDLPRLIHLIEDSFGRKLDARHYVDRINPRLAGLIIAGEYEGGAVLTWETPPGLSDDGSEEFRARMVPYLDKFAVLKRSQGAGGVADIVFNAMVRTCFPQGVCWRSRANNPVNKWYFERSRGTWKLPGTNWTMFWTTAGVPENQSRFWDYEGVCRAIEPSWADKTQQAD | Function: N-acetylglutamate synthase involved in arginine biosynthesis.
Catalytic Activity: acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate
Sequence Mass (Da): 81514
Sequence Length: 737
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
Subcellular Location: Mitochondrion
EC: 2.3.1.1
|
O75011 | MENNTASSPYTKLELVGRGSYGAVYRGICNLTKETVAIKILNLDTDEDEVSDIQKEVAVLSELKQSDVENIIKYHGSYLVGTNLWIIMDYCHGGSVRTLMEAGPISEPCISLILRETLQALKFIHHAGIIHRDIKAANILVSMSGNVKLCDFGVAAELNINRRKRITFIGTPYWMAPEVIRDGQEYNVMADIWSLGITAYEIATGSPPHAKEDPFRAVYLIAHTAPPRLNGNFSALLKEFIASCLQDVPQRRLDSSELLKSKFIKQYSRMSISELTNVVKRYDTWQAAGGIPQTLLLGEEADDGSDPDQETSDTAASDDGWEFGTIKQGQSNVSSITGTSTSTTTAATSSTTVTGTVIPKSSTVHEPPSSNDSHPLLQLFKDSKISDDDSPSNAEGASTEDSKGEVSYSQIELPSLDSSNLSSKKSTIQSKHTKQAEDYDLFVGRTRSNSKTSSDQSIKRPLPRVVQRQKTSLGKRGISMSPMKPGLRMPSSFDLQSRSISMGAFEQLSTPLEAPAHKHSAVLQPLEVNRSISIPPPKSISPSILHKPSLESASSTPKISSCSSTPKPFNSKLRAHLPPLSIGSPAVQPLANDNYDSLGVRGLNMELFNDYPGNMHNIKSVLSLEIDIVLGEMDACLKSLECNLLNRKAYNE | Function: Has a role in the regulation of cell polarity, growth and division.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 71120
Sequence Length: 652
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q4G0N4 | MTCYRGFLLGSCCRVAGGRAAALRGPGAGGPAARPRLGGDGGGRRHLGQGQPRELAGCGSRADGGFRPSRVVVVAKTTRYEFEQQRYRYAELSEEDLKQLLALKGSSYSGLLERHHIHTKNVEHIIDSLRNEGIEVRLVKRREYDEETVRWADAVIAAGGDGTMLLAASKVLDRLKPVIGVNTDPERSEGHLCLPVRYTHSFPEALQKFYRGEFRWLWRQRIRLYLEGTGINPVPVDLHEQQLSLNQHNRALNIERAHDERSEASGPQLLPVRALNEVFIGESLSSRASYYEISVDDGPWEKQKSSGLNLCTGTGSKAWSFNINRVATQAVEDVLNIAKRQGNLSLPLNRELVEKVTNEYNESLLYSPEEPKILFSIREPIANRVFSSSRQRCFSSKVCVRSRCWDACMVVDGGTSFEFNDGAIASMMINKEDELRTVLLEQ | Function: Mitochondrial NAD(+) kinase that phosphorylates NAD(+) to yield NADP(+). Can use both ATP or inorganic polyphosphate as the phosphoryl donor. Also has weak NADH kinase activity in vitro; however NADH kinase activity is much weaker than the NAD(+) kinase activity and may not be relevant in vivo.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 49433
Sequence Length: 442
Subcellular Location: Mitochondrion
EC: 2.7.1.23
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Q8C5H8 | MTCYRGFLLGSCRRVAGGRAALRGSGSGADGRRHLGHGQPRELAGGGSPADGGFRPSRVVVVAKTTRYEFEQQRYRYAELSEEDLKQLLALKGSSYSGLLERHHIHTKNVEHIIDSLRDEGIEVRLVKRREYDEETVRWADAVIAAGGDGTMLLAASKVLDRLKPVIGVNTDPERSEGHLCLPVRYTHSFPEALRRFSRGEFRWLWRQRIRLYLEGTGINPTPVDLHEQQLSLNQHSRAFNIERAHDERSEASGPQLLPVRALNEVFIGESLSSRMPYCWAVAVDNLRRDIPNLKGLASYYEISVDDGPWEKQKSSGLNLCTGTGSKAWSFNINRVAAQAVEDVLHIARRQGNLTLPLNKDLVEKVTNEYNESLLYSPEEPKILFSIREPIANRVFSSSRQRCFSSKVCVRSRCWDACMVVDGGTSFEFNDGAIASMMINKEDELRTVILEQ | Function: Mitochondrial NAD(+) kinase that phosphorylates NAD(+) to yield NADP(+). Can use both ATP or inorganic polyphosphate as the phosphoryl donor (By similarity).
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 50859
Sequence Length: 452
Subcellular Location: Mitochondrion
EC: 2.7.1.23
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Q08CZ6 | MSLCLRLLCSVCGAAALRVPLGVSSLRALSGSAEGFRPARVAVVAKTTRYEFEQQRYRSSGLSEAELRDLLALKGSSYNGLLQRYNIHSENVEHIVQSLRKEGTDVRLVKRRDYDEETVRWADAIISAGGDGTMLLAASKVQDRFKPVIGVNTDPERSEGHLCLPVRYTWSFPEALQKLYRGEFRWQWRQRIRLYLEGTGINLTPVDLHEQQLSLEQHNKAHNSQLEQKSVAVSGPQLLPVRALNEVFIGESLSSRVNYKSCKPRFTFSLHRASYYEISVDDGPWEKQKSSGLNVCTGTGSKAWSYNINKMSSQSVEELLNIVRQHKSLNVSLDSDVIQRVTNAYNDSLVYNPEEPKMFFSVREPIANRVFSSSQQRGFTSKVCVRSRCWDACMVVDGGTSFEFNDGAIVSIVMDDQDALCTVLLDD | Function: Mitochondrial NAD(+) kinase that phosphorylates NAD(+) to yield NADP(+). Can use both ATP or inorganic polyphosphate as the phosphoryl donor (By similarity).
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 48050
Sequence Length: 427
Subcellular Location: Mitochondrion
EC: 2.7.1.23
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Q3Z997 | MYKKIGIIYHPLNPAACELAVRLAAKLDSLGIENWSDSAWQADKLASKIQNTQLIVTTGGDGTILRTAHAILPHEIPILSINLGKVGFMTELSPEDAILGLEKVLAGNGWIDERNLLEAEYLPHNSAPARQFFIMNDAVVARGQIARVICVSVDINSHPFTTYKADGAIVSTATGSTGYSYAAGGPVLQPNSADIILTPILPHLGRGYSLVLPADSTIDLKVNTWHEATLSIDGFINMPVSSGDILRLRRSAKKINFIRLRPDNYFYKELDTKLKGNNESVYDR | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 31025
Sequence Length: 284
Subcellular Location: Cytoplasm
EC: 2.7.1.23
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Q86W26 | MAMAKARKPREALLWALSDLEENDFKKLKFYLRDMTLSEGQPPLARGELEGLIPVDLAELLISKYGEKEAVKVVLKGLKVMNLLELVDQLSHICLHDYREVYREHVRCLEEWQEAGVNGRYNQVLLVAKPSSESPESLACPFPEQELESVTVEALFDSGEKPSLAPSLVVLQGSAGTGKTTLARKMVLDWATGTLYPGRFDYVFYVSCKEVVLLLESKLEQLLFWCCGDNQAPVTEILRQPERLLFILDGFDELQRPFEEKLKKRGLSPKESLLHLLIRRHTLPTCSLLITTRPLALRNLEPLLKQARHVHILGFSEEERARYFSSYFTDEKQADRAFDIVQKNDILYKACQVPGICWVVCSWLQGQMERGKVVLETPRNSTDIFMAYVSTFLPPDDDGGCSELSRHRVLRSLCSLAAEGIQHQRFLFEEAELRKHNLDGPRLAAFLSSNDYQLGLAIKKFYSFRHISFQDFFHAMSYLVKEDQSRLGKESRREVQRLLEVKEQEGNDEMTLTMQFLLDISKKDSFSNLELKFCFRISPCLAQDLKHFKEQMESMKHNRTWDLEFSLYEAKIKNLVKGIQMNNVSFKIKHSNEKKSQSQNLFSVKSSLSHGPKEEQKCPSVHGQKEGKDNIAGTQKEASTGKGRGTEETPKNTYI | Function: Inhibits autoprocessing of CASP1, CASP1-dependent IL1B secretion, PYCARD aggregation and PYCARD-mediated apoptosis but not apoptosis induced by FAS or BID . Displays anti-inflammatory activity . Required for immunity against C.albicans infection (By similarity). Involved in the innate immune response by contributing to pro-inflammatory cytokine release in response to invasive bacterial infection . Contributes to T-cell-mediated inflammatory responses in the skin (By similarity). Plays a role in protection against periodontitis through its involvement in induction of IL1A via ERK activation in oral epithelial cells infected with periodontal pathogens . Exhibits both ATPase and GTPase activities .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 75032
Sequence Length: 655
Domain: The pyrin and ATP-binding domains are required to elicit cytokine release following bacterial infection.
Subcellular Location: Cytoplasm
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A0A6G9KJC3 | MTIANTPAELLASSISTLASRYAEKVQAGENADTEIASIVSACKDLDALVTPPESWNDRMAMSYTISTAIALLLNWDVFQILAAQAKPTSLETLATSCGCSKSLLRCALREAVAHRMLDELSPETYALNSRSSCLLDENKAAWIHYLTDIGLVTAAYLPKYVKSINGKIPEHSHRIALQMAFNVDETFYEFLHRKDPKRGVNFDKAMQRHIKGDAQASIESVFDFSILRPGAVVVDVGGGKGHHCIRIAKKHPHLSFIIQDYEANGPSDGEDTLPEALARRVRWQRHNFHHKQPMDGADVYLLSNILMDNTVSDCNRILTNIVDAMVPNHSVLLVDDAIDTLSEDSHSAYSSSMNLHMLSCFGTLFRTQEDWLMLFSEVAGGKLSIVSSWMIDAGRMIFALRRKF | Function: N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the benzazepine alkaloid nanangelenin A which contains an unprecedented 3,4-dihydro-1-benzazepine-2,5-dione-N-prenyl-N-acetoxy-anthranilamide scaffold . The first step of nanangelenin biosynthesis is catalyzed by the indoleamine 2,3-dioxygenase nanC which produces N-formyl-kynurenine through the catabolism of tryptophan . The two-module NRPS nanA then utilizes anthranilate (Ant) and L-kynurenine (L-Kyn) to assemble the dipeptide product nanangelenin B . The first adenylation domain of nanA (A1) loads anthranilate onto the T1 domain, while A2 loads kynurenine, generated through spontaneous nonenzymatic deformylation of the nanC-supplied N-formyl-kynurenine . The peptide bond formation between the tethered amino acids is catalyzed by the first condensation domain (C1) between anthranilate's carbonyl carbon and kynurenine's aliphatic primary amine . The second C domain (C2) catalyzes the final cyclization event between the aromatic amine of kynurenine and the tethered carbonyl carbon, yielding nanangelenin B . The terminal T3 domain enhances the catalytic efficiency of C2, suggesting the T2-tethered Ant-L-Kyn is transferred to T3 prior to cyclization by C2 . Once released from nanA, nanangelenin B is then prenylated by the prenyltransferase nanD to form nanangelenin C . Nanangelenin C is then N-hydroxylated by the FAD-dependent monooxygenase nanF and further acetylated by the acetyltransferase nanB to yield nanangelenin F . Finally, the N-methyltransferase nanE methylates the amide nitrogen of 1-benzazepine to convert nanangelenin F into nanangelenin A . NanE is also able to methylate most of the intermediates of the pathway such as nanangelenin B and nanangelenin C to produce nanangelenin D and nanangelenin E, respectively .
Sequence Mass (Da): 44974
Sequence Length: 405
Pathway: Secondary metabolite biosynthesis.
EC: 2.1.1.-
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O51589 | MIIIVKIKRGLIVSCQALENEPLHSSFIMSKMALAAKIGGAIGIRANGVNDISQIKLEVDLPIIGIIKKNYNNCDVFITPTMKEIDELCNEGVDIIALDATFRNRPDGVLLDDFFENIKKKYPKQCLMADISSLDEAINADKLGFDFIGTTLYGYTKNTNGLNIADNDFNFLRTLLNSNLKSTLIVEGKIDTPLKAQKCFEMGVDLVVVGGAITRPAEITKKFVEKINQIKK | Function: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
Catalytic Activity: an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-mannosamine 6-phosphate
Sequence Mass (Da): 25644
Sequence Length: 232
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 3/5.
EC: 5.1.3.9
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Q8R7I7 | MQMDIIQKLENGLIVSCQALEGEPLHSPFIMAKMAKAAEIGGAVAIRANGYEDIVAIKKEVSIPVIGLIKKRYEGYAPYITPTMEEVDKVIEAGADIVAIDATKAYKPGGLTTGEFLKRIKEKYPKILVMADISTYEEGIEAEKLGFDLISTTLSGYTEYSPELEGPDYELIERLARKVNVPIIAEGRIWTPEEAVKALEKGAYAVVVGTAITRPHEITRRFVTFIKERRYSNVRAK | Function: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
Catalytic Activity: an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-mannosamine 6-phosphate
Sequence Mass (Da): 26268
Sequence Length: 237
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 3/5.
EC: 5.1.3.9
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Q0TUP9 | MLDVVKGNLIVSCQALSDEPLHSSFIMGRMAIAAKQGGAAAIRAQGVNDINEIKEVTKLPIIGIIKRNYDDSEIYITPTMKEVDELLKTDCEMIALDATKRKRPNGENVKDLVDAIHAKGRLAMADISTLEEGIEAEKLGFDCVSTTLSGYTPYSKQSNSVDFELLEELVKTVKIPVICEGRINTPEELKKALDLGAYSAVVGGAITRPQQITKRFTDILK | Function: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
Catalytic Activity: an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-mannosamine 6-phosphate
Sequence Mass (Da): 24153
Sequence Length: 221
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 3/5.
EC: 5.1.3.9
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A4QH48 | MDLNTQRSKLYAQLQGQLIVSVQAPDGHAMRDTHTLTHVAAACVDGGAPAIRCGGYGGLEDIRSISNRVDVPVFGLTKEGSEGVYITPTRDSVRAVAESGATVVCADATFRPRPDGSTFAELVTVAHDSGILIMADCATPEEVLSAHKAGADFVSTTLAGYTEHREKTVGPDFDCLREARELVPDAFLIGEGRFSNPADVAHGRLIGANAIIVGTAITDPGFITGQFASLLH | Function: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
Catalytic Activity: an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-mannosamine 6-phosphate
Sequence Mass (Da): 24361
Sequence Length: 232
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 3/5.
EC: 5.1.3.9
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Q6A6A0 | MSGFTDRIIASMAGGLVVSCQAYPGEPLRHPETMAQMAAAVEAGGAVAVRAQGLSDVSAVKGRVSVPVVGIWKEGDEGIYITPTLRHARCVSAAGADVVALDGTRRERADGLSLAETIERLKREYDVVVMADCGSVDDGLFAAEAGADLIGTTLCGYTGERPKTDGPDYEVIEALVKKLDGDRPVIAEGRIHTPDQARRAMDLGAHAVVVGTAITHPTSITGWFRDALR | Function: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
Catalytic Activity: an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-mannosamine 6-phosphate
Sequence Mass (Da): 24056
Sequence Length: 229
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 3/5.
EC: 5.1.3.9
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Q9CKB3 | MRCLALDIGGTKIASAIVTDGKIEQRQQIATPQADAANAMHDTLANILALYAGQFDYVAVASTGIINHGVLTALNPKNLGGLAEFPLKESIARHTDKPIGLLNDVQAAACAEYKDEDKNAVQNFVFITVSTGVGGGIILERRLLTEPNGVAGHIGHTLADPNGPVCGCGRVGCVEAVAAGRAIEAVSSQWNPPCTPKQAFELFRKNDEKATALIQRSASAIANLIADLVIGLDVQKVVVGGSVGLAEGYLPLVKQYLNMMPHFYHCTVEQARHGQDAGLLGAAWWVADCLKQGVHLK | Function: Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P.
Catalytic Activity: an N-acyl-D-mannosamine + ATP = ADP + an N-acyl-D-mannosamine 6-phosphate + H(+)
Sequence Mass (Da): 31351
Sequence Length: 297
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 2/5.
EC: 2.7.1.60
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Q70Z17 | MSNAKDNFNVADLTAALNAEDRDDLVNVLKNKLQGLTGKHSNVLENLSPNVRKRVEVLREIQTQHDELEAKFFEERAALEAKYQKQYQPLYAKRSEIVNGVVEVDGEATQTAAADEEEDKDSVEKGVPDFWVTAMKNNEVLAEEITERDEGALKFLKDIKWSRIENPKGFKLEFFFETNPYFTNTVLTKTYHMIDEDEPILEKAIGTEIEWHPGKCLTQKILKKKPKKGSKNSKPITKIEQCESFFNFFSPPQVPDDEEDIDEDAAEELQNLMEQDYDIGSTIRDKIIPHAVSWFTGEAAQDEDYIDLEDDEDEEDDEDEDEDEEDEEEEDEDEDDDDEDEHVTKTKKKSSAGRKRSGGAPAADGQPGERPPECKQQ | Function: May modulate chromatin structure by regulation of nucleosome assembly/disassembly (By similarity). Could function together with B-type cyclins in the regulation of microtubule dynamics.
Sequence Mass (Da): 43090
Sequence Length: 377
Domain: The acidic domain is probably involved in the interaction with histones.
Subcellular Location: Nucleus
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F4JEI8 | MSNEENIKSDNKSGDSSDLPTIPALDIGAEECDLLAELKNLTLKRPFDVKKLSPKVTKRVLFLKDIQVTHDELEEKFLAEKSALEATYDNLYKPLFAKRYEIVNGVVEAEAEKEGVPNFWLIAMKTNEMLANEITERDEAALKYLKDIRSCRVEDTSRNFKLEFLFDSNLYFKNSVLSKTYHVNDEDGPVLEKVIGTDIEWFPGKCLTHKVVVKKKTKKGPKKVNNIPMTKTENCESFFNFFKPPEIPEIDEVDDYDDFDTIMTEELQNLMDQDYDIAVTIRDKLIPHAVSWFTGEALVDEDDSDDNDDDDNDEKSD | Function: May modulate chromatin structure by regulation of nucleosome assembly/disassembly.
Sequence Mass (Da): 36418
Sequence Length: 317
Domain: The acidic domain is probably involved in the interaction with histones.
Subcellular Location: Nucleus
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Q55ED1 | MSENNEIEMELPFDSSAITSTEVLDRVNALLTLQDTQNELTEQMEKEILEIEKKYLKKFQPLAEKRFEIVSGKVEPTKEDQQCKAPIQVENLKSVPTDKGIPKFWLHVLQNTEVKDIIEECDIEALEYLVDIKIVQVGDAQDYSLDFHFSENPFFTNTVISKTVKLEEDNELNEIVSTPINWKDGKNFTVQSKKKTVKSKPTKGKAATTTSTTVQEVVPCFFSTFVSPNQDPTSDEEADEIMYIQYQIIAKLKDIVIPEAVNFFLGRASDAEENDYDFGEDFEDEEGEDDDEEDDEEEQTIKKPSGKGKAQPQQPQDCKQQ | Function: May modulate chromatin structure by regulation of histone octamer formation.
Sequence Mass (Da): 36644
Sequence Length: 321
Domain: The acidic domain may be involved in the interaction with histones.
Subcellular Location: Nucleus
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P25293 | MSDPIRTKPKSSMQIDNAPTPHNTPASVLNPSYLKNGNPVRAQAQEQDDKIGTINEEDILANQPLLLQSIQDRLGSLVGQDSGYVGGLPKNVKEKLLSLKTLQSELFEVEKEFQVEMFELENKFLQKYKPIWEQRSRIISGQEQPKPEQIAKGQEIVESLNETELLVDEEEKAQNDSEEEQVKGIPSFWLTALENLPIVCDTITDRDAEVLEYLQDIGLEYLTDGRPGFKLLFRFDSSANPFFTNDILCKTYFYQKELGYSGDFIYDHAEGCEISWKDNAHNVTVDLEMRKQRNKTTKQVRTIEKITPIESFFNFFDPPKIQNEDQDEELEEDLEERLALDYSIGEQLKDKLIPRAVDWFTGAALEFEFEEDEEEADEDEDEEEDDDHGLEDDDGESAEEQDDFAGRPEQAPECKQS | Function: Acidic protein, which assembles histones into an octamer (in vitro). Involved in the regulation of the localization and the function of the septins during mitosis. Involved in the function of B-type cyclins.
PTM: Phosphorylation by CK2 is required for normal progression through S phase. CK2 phosphorylation is not required for correct bud formation nor histone binding.
Sequence Mass (Da): 47885
Sequence Length: 417
Domain: The acidic domains are probably involved in the interaction with histones.
Subcellular Location: Cytoplasm
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K4BNG7 | MVGKNNSNHLPPGFRFHPTDEELIMYYLRNQATSKPCPSSIIPEVDVYKFDPWELPEKTEFGEKEWYFFTPRDRKYPNGVRPNRAAVSGYWKATGTDKGIYSGTKYVGIKKALVFYKGKPPKGIKTDWIMHEYRLSESRTQPTRPNGSMRLDDWVLCRIYKKKNLERAIEMMKVEEDTQEPQIMSVTNPIHEVVASNGQQTLKLPRTCSLSHLLEMDYFGSISQLFDDNNSYNTISQNNTLMTNVNGYVMPHQAMEKFQLGEVSQISMNPSYQFQ | Function: Transcription factor that binds DNA motifs 5'-CGT[AG](5N)NACG[ACT][AC][AT][ACG][ACT]-3' and 5'-CACG[ACT][AC][AT][AGT][CT]-3' in target genes promoters. Promotes leaf senescence (developmental, light-induced and ABA-induced senescence) and regulates fruit yield and sugar content, probably by establishing abscisic acid (ABA) homeostasis. Activates the expression of senescence and ABA associated genes including NCED1, ABCG40, CYP707A2, SAG113, SGR1 and PAO, by directly binding to their promoters.
Sequence Mass (Da): 31877
Sequence Length: 275
Domain: The NAC domain includes a DNA binding domain and a dimerization domain.
Subcellular Location: Nucleus
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Q9ZV87 | MGKIMEWAARSDHLGGIPRNTVIMAVSAFAKAVANLCNKSSVHNADTLMNLVQSRPPGVPLITVSNHMSTLDDPVMWGAFKGLLSLDPELARWVLAAEDICFRNPIFSYIFRTGKCIPITRGGGIYQENMNEALQRLKDGSWLHTFPEGKVFQDDVPIRRLKWGTASLIARSPVTPIVLPIIHRGFEEMMPENYNNGRRPLVPLPNKHLKVVVGEPIEFDVPMMVETAVLDSRHVTPPLQEVKWPVLTSAGQVLDETAQRHLYIALSEKIQSSLETLRLLAKRL | Function: Acyltransferase that catalyzes the N-acylation of phosphatidylethanolamine to form N-acylphosphatidylethanolamine (N-acyl-PE) (e.g. NAPEs containing C16:0, C16:1, C18:0, and C18:1). Mediates also the formation of acylphosphatidylglycerol (acyl-PG) from lysoglycerophospholipid by O-acylation. Uses acyl-CoA as acyl donors. Acylates 1-acyllysophosphatidylethanolamine (1-acyllyso-PE) and 1-acyllysophosphatidylglycerol (1-acyllyso-PG) at the sn-2-position.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 31743
Sequence Length: 284
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphocholine.
Subcellular Location: Cell membrane
EC: 2.3.1.-
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P37062 | MKVIVLGSSHGGYEAVEELLNLHPDAEIQWYEKGDFISFLSCGMQLYLEGKVKDVNSVRYMTGEKMESRGVNVFSNTEITAIQPKEHQVTVKDLVSGEERVENYDKLIISPGAVPFELDIPGKDLDNIYLMRGRQWAIKLKQKTVDPEVNNVVVIGSGYIGIEAAEAFAKAGKKVTVIDILDRPLGVYLDKEFTDVLTEEMEANNITIATGETVERYEGDGRVQKIVTDKNAYDADLVVVAVGVRPNTAWLKGTLELHPNGLIKTDEYMRTSEPDVFAVGDATLIKYNPADTEVNIALATNARKQGRFAVKNLEEPVKPFPGVQGSSGLAVFDYKFASTGINEVMAQKLGKETKAVTVVEDYLMDFNPDKQKAWFKLVYDPETTQILGAQLMSKADLTANINAISLAIQAKMTIEDLAYADFFFQPAFDKPWNIINTAALEAVKQER | Cofactor: Binds 1 FAD per subunit.
Function: Peroxidase whose active site is a redox-active cysteine-sulfenic acid.
Catalytic Activity: H(+) + H2O2 + NADH = 2 H2O + NAD(+)
Sequence Mass (Da): 49566
Sequence Length: 447
EC: 1.11.1.1
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Q56348 | MIDSAKETDRPKHRKRDEVIAFLILAVVIWPILSVAIVGGYGFLVWMSQIIFGPPGPMH | Function: May be involved in mediating interactions between NapC and a quinol oxidase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6618
Sequence Length: 59
Subcellular Location: Cell inner membrane
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P0AAL2 | MKIDASRRGILTGRWRKASNGIRPPWSGDESHFLTHCTRCDACINACENNILQRGAGGYPSVNFKNNECSFCYACAQACPESLFSPRHTRAWDLQFTIGDACLAYQSVECRRCQDSCEPMAIIFRPTLSGIYQPQLNSQLCNGCGACAASCPVSAITAEYLHAH | Cofactor: Binds 3 [4Fe-4S] cluster.
Function: Could be involved in the maturation of NapA, the catalytic subunit of the periplasmic nitrate reductase, before its export into the periplasm.
Sequence Mass (Da): 18047
Sequence Length: 164
Subcellular Location: Cytoplasm
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P44650 | MTVENLPRRQFLRGKFSTLSCLENNQKQNFVGIRPPWSVENSIFVARCTRCGDCLSVCETNILVKGDAGFPEVRFDNGECTFCGKCVDACKQPIFYPRDQLPWSHKIDISVSCLTLHRIECRTCQDNCPANAIRFKLQMGGVAQPLVNFDACNGCGACVQGCPVNAITMNDLKQNE | Cofactor: Binds 4 [4Fe-4S] clusters or perhaps rather 3 [4Fe-4S] clusters and 1 3Fe-4S cluster, leaving Cys-113 out of the cluster ligands.
Function: Could be involved in the maturation of NapA, the catalytic subunit of the periplasmic nitrate reductase, before its export into the periplasm.
Sequence Mass (Da): 19604
Sequence Length: 176
Subcellular Location: Cytoplasm
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P0AAL4 | MSRSAKPQNGRRRFLRDVVRTAGGLAAVGVALGLQQQTARASGVRLRPPGAINENAFASACVRCGQCVQACPYDTLKLATLASGLSAGTPYFVARDIPCEMCEDIPCAKVCPSGALDREIESIDDARMGLAVLVDQENCLNFQGLRCDVCYRECPKIDEAITLELERNTRTGKHARFLPTVHSDACTGCGKCEKVCVLEQPAIKVLPLSLAKGELGHHYRFGWLEGNNGKS | Cofactor: Binds 4 [4Fe-4S] cluster.
Function: Required for electron transfer from ubiquinol, via NapC, to the periplasmic nitrate reductase NapAB complex.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence Mass (Da): 24925
Sequence Length: 231
Subcellular Location: Periplasm
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P44652 | MKVRLKSKKKMKKPALNPERRKFLKEATRTAGGLAGVGILLGLQQNQSLAREGVPLRPPFALQDAKAFSAACIRCGQCVQACPYDMLHLASLLSPVEAGTPYFIARDKPCEMCPDIPCAKACPSGALDRQATDINESRMGLSVLLDHETCLNYQGLRCDVCYRVCPLIDKAITLETQHNPRSDKHALFIPTVHSDACTGCGKCEQACVLEEAAIKILPMDLAKGMLGKHYRLGWEEKAKAGHSLAPKDMISLPTRTPEGTTVIPEPAEPVLAPILGSGK | Cofactor: Binds 4 [4Fe-4S] cluster.
Function: Required for electron transfer from ubiquinol, via NapC, to the periplasmic nitrate reductase NapAB complex.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence Mass (Da): 30227
Sequence Length: 279
Subcellular Location: Periplasm
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P33934 | MANRKRDAGREALEKKGWWRSHRWLVLRRLCQFFVLGMFLSGPWFGVWILHGNYSSSLLFDTVPLTDPLMTLQSLASGHLPATVALTGAVIITVLYALAGKRLFCSWVCPLNPITDLANWLRRRFDLNQSATIPRHIRYVLLVVILVGSALTGTLIWEWINPVSLMGRSLVMGFGSGALLILALFLFDLLVVEHGWCGHICPVGALYGVLGSKGVITVAATDRQKCNRCMDCFHVCPEPHVLRAPVLDEQSPVQVTSRDCMTCGRCVDVCSEDVFTITTRWSSGAKS | Cofactor: Binds 2 [4Fe-4S] cluster.
Function: Required for electron transfer from ubiquinol, via NapC, to the periplasmic nitrate reductase NapAB complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31874
Sequence Length: 287
Subcellular Location: Cell inner membrane
|
O96009 | MSPPPLLQPLLLLLPLLNVEPSGATLIRIPLHRVQPGRRILNLLRGWREPAELPKLGAPSPGDKPIFVPLSNYRDVQYFGEIGLGTPPQNFTVAFDTGSSNLWVPSRRCHFFSVPCWLHHRFDPKASSSFQANGTKFAIQYGTGRVDGILSEDKLTIGGIKGASVIFGEALWEPSLVFAFAHFDGILGLGFPILSVEGVRPPMDVLVEQGLLDKPVFSFYLNRDPEEPDGGELVLGGSDPAHYIPPLTFVPVTVPAYWQIHMERVKVGPGLTLCAKGCAAILDTGTSLITGPTEEIRALHAAIGGIPLLAGEYIILCSEIPKLPAVSFLLGGVWFNLTAHDYVIQTTRNGVRLCLSGFQALDVPPPAGPFWILGDVFLGTYVAVFDRGDMKSSARVGLARARTRGADLGWGETAQAQFPG | Function: May be involved in processing of pneumocyte surfactant precursors.
Sequence Mass (Da): 45387
Sequence Length: 420
Subcellular Location: Secreted
EC: 3.4.23.-
|
Q9N2V2 | MRISSLLFLTFLAGIVQAQDFLAMFKPFLGGGGGGGNPFANPQAIGGLFQQFAGGNGGGFGQLLAGAMAPKPAPAAAGPRSAPAPTNEDYNTDIDVPAPKAKARAAPTPRRAQADAPPVYRQPRTKAEKIERFRNIARTFSPFVYEVNTTPAPHFDNFIWQQNAPAVTPEPFTFAPFSFPTLATVAPPAPGPGGPTLEPFLPTTASPKLLAHNTARMIREIASFSDGGRSRDQDFGAVQTLMQAFFEAVSSGNNGGAGAAAGAGTALGDAPMLQAHRDGTELGANRALTNKLFESDMVLTVKQMKAIVLAAQEARNPHGRKKRKVITGSVYRWKSVIPFRFKGGDAKWKKLIREGLGLWEKETCVRWSENGPGKDYVIFFRGSGCYSSVGRTGGSQLISIGYGCEDKGIVAHEVGHSLGFWHEQSRPDRDDYIHLRKDWIIKGTDGNFEKRSWEEIEDMGVPYDVGSVMHYGSNAFTKDWDQITIETKDSRYQGTIGQRQKLSFIDVKQVNRLYCNSVCPVALPCMHGGYPDPNNCAVCKCPDGLGGKLCGRAAKGTDHDKCGGELTATAEWQEMVYKGKRTCNWKVKSPSGGRVRLVLTELRYQCAPACKAYIEIKHNTDFQQTGFRVCCFNKTYDVISDQSEALILSNANIVDYEVSYKLQWIQDNGKALPPPKPTSTWVPGKENRPFRGVENSGGTIEKFILQAIPKIRDSHRPLESITSIVAEYGLATLLGISHNGK | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
Sequence Mass (Da): 80722
Sequence Length: 741
EC: 3.4.24.-
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Q7JLI1 | MILQLLFYSLFTHLAVSQIDVNQALNQNKLNIDTISSSAISDAELEKTFPRTNLSRMRNALKSLRQNWSAKLQAMPARNYQNAGTNQENGATEQQKPLREKPRDRVKMEGDTLHQVNKAAGLNDILYQGDMVLTDDQIATILEARDETTVSTASRARRQAYRDRYYPSTTWGSSVYYYYDRTATPKIVKAFEQAVAFWQNVTCINIMQSSTAINRIRVFKGQGCYSYVGRISGVQDLSLGTGCEEFGTAAHELGHALGFFHTQSRYDRDNYISINYANIDPSYVEQFDKETSNTNFNYGMPYDYGSIMQYGATSASSNDKATMIARDTEYQDTMGSDFVGFYDISMMNEHYKCKELCPAASSAQCKNGGFPSPRNCAICICPSGYGGILCDQRPPGCGDSVTATTTWQTLTNTIGDGLPTLRDNHTMCNYWVKAPDNQAVEIRISGLTTVTIDGCIFGGVEIKTHKDQKLTGYRYCSSADQNTVHRSTGSLVPIILFNRYASTKAVLEYRAVTPSVDVSATYTTFAPIVNSCQDLHPNCDFYKFFGMCRSKKIRSNCKFTCHDCNNNNASPFGSNFFNNNYNSFNNWYTNKNKNYYPYSNSNNNKPWMWFF | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
Sequence Mass (Da): 68854
Sequence Length: 611
Subcellular Location: Secreted
EC: 3.4.24.-
|
O16977 | MRRFFICYIGFLSIFLDFILADKDNNSEEERDRKFDWKFENENGKPEHETVTVPKLPDGSYFWKWTWNSRINSTTAATPTSTVTTSTSAPTTSPRVYKLKSEARKSLRKALRGVPPEKRKKQLKKMGKKMMKIPKITKKESNKLHKSYRKVKITENPPALDMFEVNERAGLNEYLFQGDINLNNNQIAKISSEQSSKSRRKKRQIDNLAQFWPGKVVYYYFDSGLTTTVQQIVRDAITFLESNTCLKFELNSTATNRIFSGVGCYSDTGMLGGEQTLSLGYGCEVTGTAAHEIAHTLGLFHTQMRSDRDDYVTIDLTDVPESSQQNFIKLTEATSTNLVDYEYGSFMHYSGRAFVSSGGVDSIVPKDPVMVYTMGGRIVTFLDLKMLNTHYSCSCPTILSCGNGGFTNPANCSVCICPYGFGGALCTERTDYGCGSTLTATDTWQQETYTFGNASNSATARPSAVYCNHWIQAPVGKQIQFRIDSTYNTQCVYGCTFNGVEPKLKSDMTITQARYCCDEFNAEIMTADFGVNPMPVFSFNRYYKTTYTWSYRYVDSNVTACADTSDKATCLSLKSAKEQGCSIYDTAQLKVMCAATMDLCGKVASDDGTCKDRFPKSQCSTYSTNGMCTQQPPLAAEFSCAETCGFCTNPV | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
Sequence Mass (Da): 72761
Sequence Length: 651
Subcellular Location: Secreted
EC: 3.4.24.-
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P55114 | MLFVSILISQFVTCLTQPDFFERPPPPDWFFPGPLRPWGPPPPWHRNRGPPPFGPPPPWDRPPPPWRRPPWHRRPPWGLPPPPPPPEPEPQQDQPQVMFSQDIDKVVNSVNQNTAAFQRPGESYDKVIQIMSSYFNRKSGSQYDINTVIPSSGIYNNEMAANSKIAAVMFESDMALTVSQMNKVAQNGFRVKRKMNLNGTTWSRNIPYRFLDTDGNWQSQITNGLRHYERNTCIRFSLNGGGSDYLVFSKGEGCYSSVGRLGGPQEISIGDGCETLGIITHEVGHALGFWHEQARPERDSYVRINRQNAINGLEGQFDKRSWSEVNEYSLPYDYGSVMHYGPKSFSKSSTMNTVEPVDPAFINTIGNRVEPSFLDLKLLNTAFCSNICTNRINCQHGGYADPNNCGQCTCPTGLEGTYCERLQTSNCGVELPRADYSWRNISYSGSSDCYWRIVSANGGNVRFELTYVMYRCSPVCEEFVEMKAEYSHEATGYRQCCKAVLGERISKGNSVLIISKATQNSQFVLRYREDGTAPTQRPPPVRVAAPRSYSLLWSGWTRCSENCGSCGTQYRERCTSTTNCLRSAKQTRVCNTQPCAQGTTRGKRSVLQTQISHRVKRLNGWCCARFVLSRGVCVPVRTGVTHPN | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
Sequence Mass (Da): 72526
Sequence Length: 644
Subcellular Location: Secreted
EC: 3.4.24.-
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